1dfb
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STRUCTURE OF A HUMAN MONOCLONAL ANTIBODY FAB FRAGMENT AGAINST GP41 OF HUMAN IMMUNODEFICIENCY VIRUS TYPE I
OverviewOverview
The three-dimensional structure of a human monoclonal antibody (Fab), which binds specifically to a major epitope of the transmembrane protein, gp41 of the human immunodeficiency virus type 1, has been determined by, crystallographic methods to a resolution of 2.7 A. It has been previously, determined that this antibody recognizes the epitope SGKLICTTAVPWNAS, belongs to the subclass IgG1 (kappa), and exhibits antibody-dependent, cellular cytotoxicity. The quaternary structure of the Fab is in an, extended conformation with an elbow bend angle between the constant and, variable domains of 175 degrees. Structurally, four of the hypervariable, loops can be classified according to previously recognized canonical, structures. The third hypervariable loops of the heavy (H3) and light, chain (L3) are structurally distinct. Hypervariable loop H3, residues, 102H-109H, is unusually extended from the surface. The, complementarity-determining region forms a hydrophobic binding pocket that, is created primarily from hypervariable loops L3, H3, and H2.
About this StructureAbout this Structure
1DFB is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a human monoclonal antibody Fab fragment against gp41 of human immunodeficiency virus type 1., He XM, Ruker F, Casale E, Carter DC, Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7154-8. PMID:1496010
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