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dalazatide  (Alomone Labs)


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    Structured Review

    Alomone Labs dalazatide
    Structure of <t>dalazatide-bound</t> human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.
    Dalazatide, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 91 stars, based on 1 article reviews
    dalazatide - by Bioz Stars, 2026-02
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    Images

    1) Product Images from "Rearrangement of a unique Kv1.3 selectivity filter conformation upon binding of a drug"

    Article Title: Rearrangement of a unique Kv1.3 selectivity filter conformation upon binding of a drug

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.2113536119

    Structure of dalazatide-bound human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.
    Figure Legend Snippet: Structure of dalazatide-bound human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.

    Techniques Used: Cryo-EM Sample Prep



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    Structure of <t>dalazatide-bound</t> human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.
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    Structure of <t>dalazatide-bound</t> human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.
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    Structure of <t>dalazatide-bound</t> human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.
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    Image Search Results


    Structure of dalazatide-bound human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Rearrangement of a unique Kv1.3 selectivity filter conformation upon binding of a drug

    doi: 10.1073/pnas.2113536119

    Figure Lengend Snippet: Structure of dalazatide-bound human Kv1.3–Kvβ2 complex (dalazatide–Kv1.3). ( A ) Cryo-EM density map of dalazatide–Kv1.3 with fitted model viewed from the membrane plane ( Left ) and from the extracellular side ( Right ). ( B ) Dalazatide’s interactions with G448 and H451 in Kv1.3’s outer pore. The density around dalazatide is shown in magenta surface with the Kv1.3 model fitted. ( C ) Side view of EM density of the dalazatide–Kv1.3 map in white mesh with fitted model ( Left ) and surface in green ( Right ). ( D ) Distances between the carbonyl O atom of residues in the selectivity filter are shown. Only two opposite subunits are displayed for clarity. Residues in the selectivity filter are highlighted. K + ions (purple spheres) are seen at sites S2–S4; the K + ion is missing at site S1. ( E and F ) Comparison of the selectivity filter: dalazatide–Kv1.3 (dark blue) with apo-Kv1.3 ( E ) and dalazatide–Kv1.3 (orange) with KvChim (gray) ( F ). ( G ) Overlay of Y447 from apo-Kv1.3 (cyan) and dalazatide–Kv1.3 (dark blue) models with equivalent aromatic residues in the selectivity filters (shown as sticks) of Y373-KvChim (gray), F627-hERG (orange), F439-Eag-1 (purple), and Y78-KcsA (green). ( H ) Superposition of the EM density of Y447 in apo-Kv1.3 and dalazatide–Kv1.3 maps (gray mesh) with its fitted model. The position of Y447 varies by 11.8 Å in the two structures.

    Article Snippet: Dalazatide was purchased from Alomone Labs (Jerusalem, Israel).

    Techniques: Cryo-EM Sample Prep