Backbone and C beta Assignments of the Anti-gp120 Antibody Fv Fragment Complexed
with an Antigenic Peptide

System MW is the MW of the labeled Fv + unlabeled peptide

Chain L, Nmr Structure Of The 0.5b Anti-Hiv Antibody Complex With The Gp120 V3 Peptide

The 24-amino-acid peptide RP135 (NNTRKSIRIQRGPGRAFVTIGKIG) corresponds in its
amino acid sequence to the principal neutralizing determinant of the human
immunodeficiency virus type-1, IIIB isolate (HIV-1IIIB, residues 308-331 of the
envelope glycoprotein gp120). In order to map the antigenic determinant
recognized by 0.5 beta, the complex of RP135 with an anti-gp120 HIV
neutralizing antibody, 0.5 beta, which cross reacts with the peptide, was
studied by using two-dimensional NMR spectroscopy. A combination of homonuclear
Hartmann Hahn two-dimensional experiment and roating-frame Overhauser
enhancement spectroscopy of the Fab/peptide complex measured in H2O was used to
eliminate the resonances of the Fab and the tightly bound peptide residues and
to obtain sequential assignments for those parts of the peptide which retain
considerable mobility upon binding. In this manner, a total of 14 residues
(Ser6-Thr19) were shown to be part of the antigenic determinant recognized by
the antibody 0.5 beta. Lys5 and Ile20 were found to retain considerable
mobility in the bound peptide while their amide protons undergo significant
change in chemical shift upon binding. This observation suggests that these two
residues are at the boundaries of the determinant recognized by the antibody.
Competitive binding experiments using truncated peptides strongly support the
NMR observations.

Zvi, A., Kustanovich, I., Levy, R., Matsushita, M., Richalet-Secordel, P.,
Regenmortel, M. H. V., and Anglister, J., Mapping of the Antigenic
Determinant Recognized by an Anti-Gp120 HIV Neutralizing Antibody by
Two-Dimensional NMR. Eur. J. Biochem. 119: 178-187 (1995).

NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody.

Crystal Structure Of The Fab Fragment Of The Mouse Anti- Human Fas Antibody Hfe7a

Nmr Structure Of The 0.5b Anti-hiv Antibody Complex With The Gp120 V3 Peptide

immunoglobulin light chain variable region [Mus musculus]

variable region of immunoglobulin kappa light chain [Mus musculus]

immunoglobulin kappa light chain [Mus musculus]

immunoglobulin light chain, partial [Mus musculus domesticus]

immunoglobulin kappa light chain, variable region, partial [Mus musculus]

immunoglobulin kappa light chain variable region, partial [Mus musculus]

Ig kappa chain V region - mouse (fragment)

RecName: Full=Ig kappa chain V-III region PC 7043

RecName: Full=Ig kappa chain V-III region PC 6308

The assignment are reported for the Fv complexed
with an antigenic peptide comprising the full
epitope of the V3 loop of gp120 (HIV-1).
Only the backbone chemical shifts of the isotope-
labelled Fv are submitted. The unlabeled peptide
is being currently assigned and investigated by
isotope-filtering NMR techniques.

The Fv consists of two non-covalently linked chains marked
in this submission by segments L (light chain) and H (heavy
chain). The chemical shifts of the two chains are given in
separate loops. The numbering of the residues for the whole
Fv may be either sequential (1-231) or chain-specific: 1-112
for the light chain and 1-119 for the heavy chain. The second
type of numbering is submitted as the author sequence code.