1ce4
From Proteopedia
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| - | [[Image:1ce4.gif|left|200px]] | + | [[Image:1ce4.gif|left|200px]] |
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| - | '''CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1''' | + | {{Structure |
| + | |PDB= 1ce4 |SIZE=350|CAPTION= <scene name='initialview01'>1ce4</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CE4 is a [ | + | 1CE4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7589496 7589496] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Borremans, F A.M.]] | [[Category: Borremans, F A.M.]] | ||
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[[Category: hiv infection]] | [[Category: hiv infection]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:11 2008'' |
Revision as of 08:23, 20 March 2008
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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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