1ce4
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(New page: 200px<br /> <applet load="1ce4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ce4" /> '''CONFORMATIONAL MODEL FOR THE CONSENSUS V3 L...)
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Revision as of 11:50, 8 November 2007
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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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