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Structure of a human monoclonal antibody Fab fragment against gp41 of human immunodeficiency virus type 1The 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 deg. 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.
Document ID
19930048853
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
He, Xiao M.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Rueker, Florian
(Univ. of Agriculture and Forestry Vienna, Austria)
Casale, Elena
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Carter, Daniel C.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Date Acquired
August 16, 2013
Publication Date
August 1, 1992
Publication Information
Publication: National Academy of Sciences, Proceedings
ISSN: 0027-8424
Subject Category
Life Sciences (General)
Accession Number
93A32850
Funding Number(s)
PROJECT: RTOP 674-23-08-17
PROJECT: FFWF PROJECT P-7556-BIO
Distribution Limits
Public
Copyright
Other

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