1ce4: Difference between revisions

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[[Image:1ce4.gif|left|200px]]
[[Image:1ce4.gif|left|200px]]


{{Structure
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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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'''CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1'''
'''CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1'''
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==About this Structure==
==About this Structure==
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].  
1CE4 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE4 OCA].  


==Reference==
==Reference==
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[[Category: Fant, F.]]
[[Category: Fant, F.]]
[[Category: Vranken, W F.]]
[[Category: Vranken, W F.]]
[[Category: amphipathic helix]]
[[Category: Amphipathic helix]]
[[Category: hiv infection]]
[[Category: Hiv infection]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:37:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:19:51 2008''

Revision as of 09:37, 2 May 2008

File:1ce4.gif

Template:STRUCTURE 1ce4

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. 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 Page seeded by OCA on Fri May 2 12:37:43 2008

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