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PDBsum entry 1jdk
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Viral protein
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PDB id
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1jdk
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References listed in PDB file
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Key reference
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Title
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Structural and immunological characterisation of heteroclitic peptide analogues corresponding to the 600-612 region of the HIV envelope gp41 glycoprotein.
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Authors
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A.P.Du,
D.Limal,
V.Semetey,
H.Dali,
M.Jolivet,
C.Desgranges,
M.T.Cung,
J.P.Briand,
M.C.Petit,
S.Muller.
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Ref.
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J Mol Biol, 2002,
323,
503-521.
[DOI no: ]
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PubMed id
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Abstract
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The conformational and immunological properties of different analogues
corresponding to the 600-612 disulfide loop of the human immunodeficiency virus
(HIV) gp41 glycoprotein envelope were studied. Fourteen analogues were designed
and synthesised; namely, a series of seven analogues in which the disulfide bond
was replaced by a lactam bridge and a series of seven analogues in which one
residue of each analogue at a time, was replaced by its corresponding
homologised alpha-amino acid (beta(3)-amino acid). In the case of the lactam
analogues, the influence of the two possible CO-NH and NH-CO orientations of the
lactam bridge as well as the size of the lactam ring was explored. The analogues
were tested in ELISA with monoclonal antibodies raised against the 600-612
cyclic parent peptide as well as with sera from HIV-1 infected patients. A
structural analysis of the parent and analogue peptides was carried out in
dimethyl sulfoxide (DMSO-d(6)) using two-dimensional NMR techniques and
molecular dynamics simulations. Comparison of the own conformation of the cyclic
analogues with their either strong or weak reactivity with the antibodies
reveals structural features that may be correlated with the antibody reactivity.
Thus, a close structural similarity, particularly a characteristic orientation
of the side-chains of residues Lys606, Leu607 and Ile608 in the loop, was found
in certain beta(3)-analogues that were better recognised than the parent peptide
by anti-peptide mouse monoclonal antibodies and patients' antibodies.
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