2bf1

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(New page: 200px<br /><applet load="2bf1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bf1, resolution 4.00&Aring;" /> '''STRUCTURE OF AN UNLI...)
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[[Image:2bf1.gif|left|200px]]<br /><applet load="2bf1" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bf1.gif|left|200px]]<br /><applet load="2bf1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bf1, resolution 4.00&Aring;" />
caption="2bf1, resolution 4.00&Aring;" />
'''STRUCTURE OF AN UNLIGANDED AND FULLY-GLYCOSYLATED SIV GP120 ENVELOPE GLYCOPROTEIN'''<br />
'''STRUCTURE OF AN UNLIGANDED AND FULLY-GLYCOSYLATED SIV GP120 ENVELOPE GLYCOPROTEIN'''<br />
==Overview==
==Overview==
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Envelope glycoproteins of human and simian immunodeficiency virus (HIV and, SIV) undergo a series of conformational changes when they interact with, receptor (CD4) and co-receptor on the surface of a potential host cell, leading ultimately to fusion of viral and cellular membranes. Structures, of fragments of gp120 and gp41 from the envelope protein are known, in, conformations corresponding to their post-attachment and postfusion, states, respectively. We report the crystal structure, at 4 A resolution, of a fully glycosylated SIV gp120 core, in a conformation representing its, prefusion state, before interaction with CD4. Parts of the protein have a, markedly different organization than they do in the CD4-bound state., Comparison of the unliganded and CD4-bound structures leads to a model for, events that accompany receptor engagement of an envelope glycoprotein, trimer. The two conformations of gp120 also present distinct antigenic, surfaces. We identify the binding site for a compound that inhibits viral, entry.
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Envelope glycoproteins of human and simian immunodeficiency virus (HIV and SIV) undergo a series of conformational changes when they interact with receptor (CD4) and co-receptor on the surface of a potential host cell, leading ultimately to fusion of viral and cellular membranes. Structures of fragments of gp120 and gp41 from the envelope protein are known, in conformations corresponding to their post-attachment and postfusion states, respectively. We report the crystal structure, at 4 A resolution, of a fully glycosylated SIV gp120 core, in a conformation representing its prefusion state, before interaction with CD4. Parts of the protein have a markedly different organization than they do in the CD4-bound state. Comparison of the unliganded and CD4-bound structures leads to a model for events that accompany receptor engagement of an envelope glycoprotein trimer. The two conformations of gp120 also present distinct antigenic surfaces. We identify the binding site for a compound that inhibits viral entry.
==About this Structure==
==About this Structure==
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2BF1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_immunodeficiency_virus Simian immunodeficiency virus] with NAG and MAN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BF1 OCA].
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2BF1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_immunodeficiency_virus Simian immunodeficiency virus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=MAN:'>MAN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF1 OCA].
==Reference==
==Reference==
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[[Category: Chen, B.]]
[[Category: Chen, B.]]
[[Category: Gong, H.]]
[[Category: Gong, H.]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
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[[Category: Skehel, J.J.]]
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[[Category: Skehel, J J.]]
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[[Category: Vogan, E.M.]]
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[[Category: Vogan, E M.]]
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[[Category: Wiley, D.C.]]
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[[Category: Wiley, D C.]]
[[Category: MAN]]
[[Category: MAN]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: siv]]
[[Category: siv]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:46:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:06 2008''

Revision as of 14:37, 21 February 2008


2bf1, resolution 4.00Å

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STRUCTURE OF AN UNLIGANDED AND FULLY-GLYCOSYLATED SIV GP120 ENVELOPE GLYCOPROTEIN

Overview

Envelope glycoproteins of human and simian immunodeficiency virus (HIV and SIV) undergo a series of conformational changes when they interact with receptor (CD4) and co-receptor on the surface of a potential host cell, leading ultimately to fusion of viral and cellular membranes. Structures of fragments of gp120 and gp41 from the envelope protein are known, in conformations corresponding to their post-attachment and postfusion states, respectively. We report the crystal structure, at 4 A resolution, of a fully glycosylated SIV gp120 core, in a conformation representing its prefusion state, before interaction with CD4. Parts of the protein have a markedly different organization than they do in the CD4-bound state. Comparison of the unliganded and CD4-bound structures leads to a model for events that accompany receptor engagement of an envelope glycoprotein trimer. The two conformations of gp120 also present distinct antigenic surfaces. We identify the binding site for a compound that inhibits viral entry.

About this Structure

2BF1 is a Single protein structure of sequence from Simian immunodeficiency virus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of an unliganded simian immunodeficiency virus gp120 core., Chen B, Vogan EM, Gong H, Skehel JJ, Wiley DC, Harrison SC, Nature. 2005 Feb 24;433(7028):834-41. PMID:15729334

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