1b03

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(New page: 200px<br /> <applet load="1b03" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b03" /> '''SOLUTION STRUCTURE OF THE ANTIBODY-BOUND HI...)
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'''SOLUTION STRUCTURE OF THE ANTIBODY-BOUND HIV-1IIIB V3 PEPTIDE'''<br />
'''SOLUTION STRUCTURE OF THE ANTIBODY-BOUND HIV-1IIIB V3 PEPTIDE'''<br />
==Overview==
==Overview==
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The refined solution structure of an 18-residue HIV-1IIIB V3 peptide in, complex with the Fv fragment of an anti-gp120 antibody reveals an, unexpected type VI beta-turn comprising residues RGPG at the center of a, beta-hairpin. The central glycine and proline of this turn are linked by a, cis peptide bond. The residues of the turn interact extensively with the, antibody Fv. 15N[1H] NOE measurements show that the backbone of the, peptide, including the central QRGPGR loop, is well ordered in the, complex. The solution structure is significantly different from the X-ray, structures of HIV-1MN V3 peptides bound to anti-peptide antibodies. These, differences could be due to a two-residue (QR) insertion preceding the, GPGR sequence in the HIV-1IIIB strain, and the much longer peptide epitope, immobilized by the anti-gp120 antibody.
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The refined solution structure of an 18-residue HIV-1IIIB V3 peptide in complex with the Fv fragment of an anti-gp120 antibody reveals an unexpected type VI beta-turn comprising residues RGPG at the center of a beta-hairpin. The central glycine and proline of this turn are linked by a cis peptide bond. The residues of the turn interact extensively with the antibody Fv. 15N[1H] NOE measurements show that the backbone of the peptide, including the central QRGPGR loop, is well ordered in the complex. The solution structure is significantly different from the X-ray structures of HIV-1MN V3 peptides bound to anti-peptide antibodies. These differences could be due to a two-residue (QR) insertion preceding the GPGR sequence in the HIV-1IIIB strain, and the much longer peptide epitope immobilized by the anti-gp120 antibody.
==About this Structure==
==About this Structure==
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1B03 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=1B03 OCA].
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1B03 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=1B03 OCA].
==Reference==
==Reference==
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[[Category: p1053 structure]]
[[Category: p1053 structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:52:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:05 2008''

Revision as of 09:50, 21 February 2008


1b03

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SOLUTION STRUCTURE OF THE ANTIBODY-BOUND HIV-1IIIB V3 PEPTIDE

Overview

The refined solution structure of an 18-residue HIV-1IIIB V3 peptide in complex with the Fv fragment of an anti-gp120 antibody reveals an unexpected type VI beta-turn comprising residues RGPG at the center of a beta-hairpin. The central glycine and proline of this turn are linked by a cis peptide bond. The residues of the turn interact extensively with the antibody Fv. 15N[1H] NOE measurements show that the backbone of the peptide, including the central QRGPGR loop, is well ordered in the complex. The solution structure is significantly different from the X-ray structures of HIV-1MN V3 peptides bound to anti-peptide antibodies. These differences could be due to a two-residue (QR) insertion preceding the GPGR sequence in the HIV-1IIIB strain, and the much longer peptide epitope immobilized by the anti-gp120 antibody.

About this Structure

1B03 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

A cis proline turn linking two beta-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide., Tugarinov V, Zvi A, Levy R, Anglister J, Nat Struct Biol. 1999 Apr;6(4):331-5. PMID:10201400

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