35 research outputs found

    Structure of the llama heavy chain antibody fragment V<sub>HH</sub> D7.

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    <p>(<b>A</b>) Ribbon representation of D7; the complementarity determining regions (CDR) are highlighted in yellow (CDR1), orange (CDR2) and salmon (CDR3). The first and last residue of each CDR is shown together with the side chain of Trp<sup>96</sup> critical for gp120 interaction and neutralization. The dotted line indicates CDR3 residues lacking continuous main chain density for residues Arg<sup>100</sup> to Ser<sup>100B</sup>. (<b>B</b>) A close-up of the CDR interaction network reveals multiple polar interactions between CDR1 and CDR3 as well as CDR2 and CDR3.</p

    Comparison of CDR2 and CDR3 from D7, b12, b13, F105 and m18 indicates different modes of gp120 interaction.

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    <p>The Cα atoms of the heavy chain variable domains (b12 pdb code 2NY7; F105 pdb code 3HI1; b13 pdb code 3IDX; m18 pdb code 2AJ3) were superimposed and the CDR H2 and H3 are represented in the same orientation. Amino acids are labelled using the one letter code for clarity. (<b>A</b>) All CDR3 loops expose aromatic residues at their apex. (<b>B</b>) The CDR2 of D7 varies from CDR H2 of b12 indicating a different mode of gp120 interaction. Residues implicated in gp120 interaction are highlighted in orange.</p
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