1DFB

STRUCTURE OF A HUMAN MONOCLONAL ANTIBODY FAB FRAGMENT AGAINST GP41 OF HUMAN IMMUNODEFICIENCY VIRUS TYPE I

Summary for 1DFB

• Entry DOI: 10.2210/pdb1dfb/pdb
• Descriptor: IGG1-KAPPA 3D6 FAB (LIGHT CHAIN), IGG1-KAPPA 3D6 FAB (HEAVY CHAIN) (2 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 47714.25

Authors

He, X.M.,Rueker, F.,Casale, E.,Carter, D.C. (deposition date: 1992-03-27, release date: 1993-10-31, Last modification date: 2024-10-16)

Primary citation

He, X.M.,Ruker, F.,Casale, E.,Carter, D.C.
Structure of a human monoclonal antibody Fab fragment against gp41 of human immunodeficiency virus type 1.
Proc.Natl.Acad.Sci.USA, 89:7154-7158, 1992

PubMed Abstract: 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.

PubMed: 1496010
DOI: 10.1073/pnas.89.15.7154

Experimental method

X-RAY DIFFRACTION (2.7 Å)