1ce4
From Proteopedia
(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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'''CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1'''<br /> | '''CONFORMATIONAL MODEL FOR THE CONSENSUS V3 LOOP OF THE ENVELOPE PROTEIN GP120 OF HIV-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The disulfide bridge closed cyclic peptide corresponding to the whole | + | 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== | ==About this Structure== | ||
| - | 1CE4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1CE4 is a [http://en.wikipedia.org/wiki/Single_protein 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7589496 7589496] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7589496 7589496] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Borremans, F | + | [[Category: Borremans, F A.M.]] |
[[Category: Budesinsky, M.]] | [[Category: Budesinsky, M.]] | ||
[[Category: Fant, F.]] | [[Category: Fant, F.]] | ||
| - | [[Category: Vranken, W | + | [[Category: Vranken, W F.]] |
[[Category: amphipathic helix]] | [[Category: amphipathic helix]] | ||
[[Category: hiv infection]] | [[Category: hiv infection]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:06 2008'' |
Revision as of 10:05, 21 February 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
Page seeded by OCA on Thu Feb 21 12:05:06 2008
