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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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'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CE4 OCA].
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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]]
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[[Category: Borremans, F.A.M.]]
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[[Category: Borremans, F A.M.]]
[[Category: Budesinsky, M.]]
[[Category: Budesinsky, M.]]
[[Category: Fant, F.]]
[[Category: Fant, F.]]
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[[Category: Vranken, W.F.]]
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[[Category: Vranken, W F.]]
[[Category: amphipathic helix]]
[[Category: amphipathic helix]]
[[Category: hiv infection]]
[[Category: hiv infection]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:56:49 2007''
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''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


1ce4

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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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