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Image Search Results
Journal: Nature Communications
Article Title: Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9
doi: 10.1038/s41467-023-38509-2
Figure Lengend Snippet: a Buried surface area (BSA) contributions of individual residues to rsCSP binding in the L9 heavy chain. Sequence alignment to the IGHV3-33 germline gene shown below. b Same as in a, for the L9 light chain. c , d Structural details of NPNV binding. e NPNA 2 epitope structure in the NPNA-specific mAb 2243 (PBD 6O23), highlighting the two key CH-π interactions of germline-encoded aromatic residues (W52 H and Y94 L ) with the repeat prolines. f Same as in e, with X-ray structures of six NPNA-specific mAbs superimposed to highlight structural conservation. These six mAbs are shown in g . g Electrostatic surface potentials from L9 cryo-EM structure +/− peptide (upper left two panels) and X-ray structures of six other NPNA-specific mAbs bound to peptide; electrostatic potentials were calculated in PyMol . The PDB accession codes are in parentheses. K b : Boltzmann constant; T : temperature in kelvin; c e : electron charge in coulombs. Source data are provided as a Source Data file.
Article Snippet:
Techniques: Binding Assay, Sequencing, Cryo-EM Sample Prep
Journal: Nature Communications
Article Title: Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9
doi: 10.1038/s41467-023-38509-2
Figure Lengend Snippet: a Ribbon diagram of Fab B (cyan) and C (maroon); side chains of interacting residues are shown. b – d Structural details of key homotypic interactions. Dashed lines indicate specific contacts. e Buried surface area (BSA) contributions of individual residues to the homotypic interface in L9 light chain. Sequence alignment with F10 K and germline IGKV1-5 gene is shown below. f Same as in e , for L9 heavy chain, with sequence alignment to F10 H and germline IGHV3-33 gene. Source data are provided as a Source Data file.
Article Snippet:
Techniques: Sequencing