s1133 sigma c protein structure Search Results


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    Millipore s1133 sigma c protein structure
    Conserved and variable regions of predicted antigenic epitopes of the <t>Sigma</t> C protein shown on the modelled Sigma C carboxy terminus receptor binding domain trimeric structure. ( a and b ) Conserved proposed receptor binding residues. The conserved residues are highlighted in red as “cartoons”. ( c to h ) The conserved amino acid residues on the predicted antigenic epitopes between the <t>S1133</t> vaccine strain and our isolates which grouped into different cluster “C” groups are shown in green as “surface” on the carobxy terminus receptor binding domain model structure of the Sigma C protein. The variable regions are shown in yellow. * 194 DV substituted by 194 VM, ** 260 M substituted by I, *** 294 T substituted by N or A and **** 294 A substituted by N or D in some cases.
    S1133 Sigma C Protein Structure, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Conserved and variable regions of predicted antigenic epitopes of the Sigma C protein shown on the modelled Sigma C carboxy terminus receptor binding domain trimeric structure. ( a and b ) Conserved proposed receptor binding residues. The conserved residues are highlighted in red as “cartoons”. ( c to h ) The conserved amino acid residues on the predicted antigenic epitopes between the S1133 vaccine strain and our isolates which grouped into different cluster “C” groups are shown in green as “surface” on the carobxy terminus receptor binding domain model structure of the Sigma C protein. The variable regions are shown in yellow. * 194 DV substituted by 194 VM, ** 260 M substituted by I, *** 294 T substituted by N or A and **** 294 A substituted by N or D in some cases.

    Journal: Scientific Reports

    Article Title: Phenotypic, genotypic and antigenic characterization of emerging avian reoviruses isolated from clinical cases of arthritis in broilers in Saskatchewan, Canada

    doi: 10.1038/s41598-017-02743-8

    Figure Lengend Snippet: Conserved and variable regions of predicted antigenic epitopes of the Sigma C protein shown on the modelled Sigma C carboxy terminus receptor binding domain trimeric structure. ( a and b ) Conserved proposed receptor binding residues. The conserved residues are highlighted in red as “cartoons”. ( c to h ) The conserved amino acid residues on the predicted antigenic epitopes between the S1133 vaccine strain and our isolates which grouped into different cluster “C” groups are shown in green as “surface” on the carobxy terminus receptor binding domain model structure of the Sigma C protein. The variable regions are shown in yellow. * 194 DV substituted by 194 VM, ** 260 M substituted by I, *** 294 T substituted by N or A and **** 294 A substituted by N or D in some cases.

    Article Snippet: Structure modelling and antigenicity prediction A blast search in PDB protein data bank using Sigma C protein sequences of our ARV isolates produced the S1133 Sigma C protein structure [PDB 2jjl] as the first hit and was chosen as a template structure.

    Techniques: Binding Assay

    ( a ) A multiple amino acid sequence alignment of the common American vaccine strain S1133 and the 28 ARV field isolates. The alignment was made by a ClustalW alignment with BLOSUM cost matrix technique. Disagreements to the consensus sequence are highlighted. ( b ) Mapping of Dde I, Hinc II, Taq aI, Bcn I and Hae III restriction sites on Sigma C sequences of the ARV isolates (i.e. one isolate from each cluster group SK-R23 [Cluster II], SK-R16 [Cluster IV], SK-R10 [Cluster V], SK-R3 [Cluster VI]).

    Journal: Scientific Reports

    Article Title: Phenotypic, genotypic and antigenic characterization of emerging avian reoviruses isolated from clinical cases of arthritis in broilers in Saskatchewan, Canada

    doi: 10.1038/s41598-017-02743-8

    Figure Lengend Snippet: ( a ) A multiple amino acid sequence alignment of the common American vaccine strain S1133 and the 28 ARV field isolates. The alignment was made by a ClustalW alignment with BLOSUM cost matrix technique. Disagreements to the consensus sequence are highlighted. ( b ) Mapping of Dde I, Hinc II, Taq aI, Bcn I and Hae III restriction sites on Sigma C sequences of the ARV isolates (i.e. one isolate from each cluster group SK-R23 [Cluster II], SK-R16 [Cluster IV], SK-R10 [Cluster V], SK-R3 [Cluster VI]).

    Article Snippet: Structure modelling and antigenicity prediction A blast search in PDB protein data bank using Sigma C protein sequences of our ARV isolates produced the S1133 Sigma C protein structure [PDB 2jjl] as the first hit and was chosen as a template structure.

    Techniques: Sequencing