2l87

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'''Unreleased structure'''
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[[Image:2l87.jpg|left|200px]]
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The entry 2l87 is ON HOLD until Paper Publication
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{{STRUCTURE_2l87| PDB=2l87 | SCENE= }}
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Authors: Schnur, E., Noah, E., Ayzenshtat, I., Sargsyan, H., Inuib, T., Ding, F., Arshava, B., Sagi, Y., Kessler, N., Levy, R., Scherf, T., Naider, F., Anglister, J.
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===The 27-residue N-terminus CCR5-peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide===
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Description: The 27-residue N-terminus CCR5-peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide
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The line below this paragraph, {{ABSTRACT_PUBMED_21763489}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 21763489 is the PubMed ID number.
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{{ABSTRACT_PUBMED_21763489}}
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==About this Structure==
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[[2l87]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L87 OCA].
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==Reference==
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<ref group="xtra">PMID:021763489</ref><references group="xtra"/>
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[[Category: Anglister, J.]]
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[[Category: Arshava, B.]]
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[[Category: Ayzenshtat, I.]]
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[[Category: Ding, F X.]]
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[[Category: Inui, T.]]
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[[Category: Kessler, N.]]
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[[Category: Levy, R.]]
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[[Category: Naider, F.]]
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[[Category: Noah, E.]]
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[[Category: Sagi, Y.]]
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[[Category: Sargsyan, H.]]
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[[Category: Scherf, T.]]
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[[Category: Schnur, E.]]
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[[Category: Helix]]
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[[Category: Hiv co-receptor]]
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[[Category: Signaling protein]]

Revision as of 06:09, 27 July 2011

Image:2l87.jpg

Template:STRUCTURE 2l87

The 27-residue N-terminus CCR5-peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide

Template:ABSTRACT PUBMED 21763489

About this Structure

2l87 is a 1 chain structure. Full experimental information is available from OCA.

Reference

  • Schnur E, Noah E, Ayzenshtat I, Sargsyan H, Inui T, Ding FX, Arshava B, Sagi Y, Kessler N, Levy R, Scherf T, Naider F, Anglister J. The Conformation and Orientation of a 27-Residue CCR5 Peptide in a Ternary Complex with HIV-1 gp120 and a CD4-Mimic Peptide. J Mol Biol. 2011 Jul 29;410(5):778-97. PMID:21763489 doi:10.1016/j.jmb.2011.04.023

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OCA

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