1ce4
From Proteopedia
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+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ce4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce4 OCA], [http://www.ebi.ac.uk/pdbsum/1ce4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ce4 RCSB]</span> | ||
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[[Category: hiv infection]] | [[Category: hiv infection]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:51 2008'' |
Revision as of 16:19, 30 March 2008
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1
Overview
The disulfide bridge closed cyclic peptide corresponding to the whole Consensus V3 loop of the envelope protein gp120 of HIV-1 was examined by proton 2D-NMR spectroscopy in water and in a 20% trifluoroethanol/water solution. In water, NOE data support a beta-turn conformation for the central conservative GPGR region and point towards partial formation of a helix in the C-terminal part. Upon addition of trifluoroethanol, a C-terminal helix is formed. This is evidenced by NOE data, alpha-proton chemical shift changes and changes in the JN alpha vicinal coupling constants. The C-terminal helix is amphipathic and also occurs in other examined strains. It could therefore be an important feature for the functioning of the V3 loop.
About this Structure
1CE4 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
The complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution., Vranken WF, Budesinsky M, Fant F, Boulez K, Borremans FA, FEBS Lett. 1995 Oct 23;374(1):117-21. PMID:7589496
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