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| - | [[Image:1ai1.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ai1.png|left|200px]] |
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| | {{STRUCTURE_1ai1| PDB=1ai1 | SCENE= }} | | {{STRUCTURE_1ai1| PDB=1ai1 | SCENE= }} |
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| - | '''HIV-1 V3 LOOP MIMIC'''
| + | ===HIV-1 V3 LOOP MIMIC=== |
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| - | ==Overview==
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| - | Antigenic variation among different HIV-1 isolates has been a major problem in the development of an effective vaccine against AIDS. Peptide vaccines incorporating structural elements common to groups of viral isolates, such as the clade subtypes of HIV-1, hold promise; however, the design of such immunogens has been hampered by the lack of specific structural information on the viral proteins to be targeted. As part of a structure-based approach to this problem, we report the design and characterization of a conformationally restricted peptide analog (Aib142) of a highly conserved HIV-1 clade-B sequence from the third variable loop of the membrane glycoprotein gp120. The design strategy incorporates peptide conformational data derived from crystal structure analysis of an MN-isolate peptide (RP142) in complex with the Fab fragment (Fab59.1) of a broadly neutralizing antibody. The synthetic peptide (Aib142) replaces an alanine residue within the V3 loop epitope sequence GPGRAF by the conformationally restricted helicogenic alpha-aminoisobutyryl residue. As expected, the crystal structure of the Fab 59.1-Aib142 complex at 2.8 A resolution shows that the peptide interacts very similarly with the neutralizing antibody. Proton nuclear magnetic resonance (NMR) studies indicate that the free Aib142 peptide is indeed more ordered in solution with a conformational preference that corresponds to the X-ray structure of its Fab-bound form. Aib142 thus represents the first step in the design of conformationally constrained peptide analogs built to mimic biologically relevant structural forms of HIV-1 neutralization sites.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9054968}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9054968 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9054968}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Constrained hiv-1 v3 loop peptide]] | | [[Category: Constrained hiv-1 v3 loop peptide]] |
| | [[Category: Immunoglobulin]] | | [[Category: Immunoglobulin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:17:43 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:53:33 2008'' |
Revision as of 13:53, 30 June 2008
Template:STRUCTURE 1ai1
HIV-1 V3 LOOP MIMIC
Template:ABSTRACT PUBMED 9054968
About this Structure
1AI1 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization site., Ghiara JB, Ferguson DC, Satterthwait AC, Dyson HJ, Wilson IA, J Mol Biol. 1997 Feb 14;266(1):31-9. PMID:9054968
Page seeded by OCA on Mon Jun 30 16:53:33 2008
