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1hiw

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(New page: 200px<br /> <applet load="1hiw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hiw, resolution 2.3&Aring;" /> '''TRIMERIC HIV-1 MATRI...)
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[[Image:1hiw.gif|left|200px]]<br />
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[[Image:1hiw.gif|left|200px]]<br /><applet load="1hiw" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1hiw" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1hiw, resolution 2.3&Aring;" />
caption="1hiw, resolution 2.3&Aring;" />
'''TRIMERIC HIV-1 MATRIX PROTEIN'''<br />
'''TRIMERIC HIV-1 MATRIX PROTEIN'''<br />
==Overview==
==Overview==
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The human immunodeficiency virus type 1 (HIV-1) matrix protein forms a, structural shell associated with the inner viral membrane and performs, other essential functions throughout the viral life cycle. The crystal, structure of the HIV-1 matrix protein, determined at 2.3 angstrom, resolution, reveals that individual matrix molecules are composed of five, major helices capped by a three-stranded mixed beta-sheet. Unexpectedly, the protein assembles into a trimer in three different crystal lattices, burying 1880 angstrom2 of accessible surface area at the trimer, interfaces. Trimerization appears to create a large, bipartite membrane, binding surface in which exposed basic residues could cooperate with the, N-terminal myristoyl groups to anchor the protein on the acidic inner, membrane of the virus.
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The human immunodeficiency virus type 1 (HIV-1) matrix protein forms a structural shell associated with the inner viral membrane and performs other essential functions throughout the viral life cycle. The crystal structure of the HIV-1 matrix protein, determined at 2.3 angstrom resolution, reveals that individual matrix molecules are composed of five major helices capped by a three-stranded mixed beta-sheet. Unexpectedly, the protein assembles into a trimer in three different crystal lattices, burying 1880 angstrom2 of accessible surface area at the trimer interfaces. Trimerization appears to create a large, bipartite membrane binding surface in which exposed basic residues could cooperate with the N-terminal myristoyl groups to anchor the protein on the acidic inner membrane of the virus.
==About this Structure==
==About this Structure==
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1HIW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HIW OCA].
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1HIW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIW OCA].
==Reference==
==Reference==
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[[Category: Human immunodeficiency virus]]
[[Category: Human immunodeficiency virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bancroft, D.P.]]
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[[Category: Bancroft, D P.]]
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[[Category: Christensen, A.M.]]
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[[Category: Christensen, A M.]]
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[[Category: Hill, C.P.]]
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[[Category: Hill, C P.]]
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[[Category: Sundquist, W.I.]]
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[[Category: Sundquist, W I.]]
[[Category: Worthylake, D.]]
[[Category: Worthylake, D.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: p17]]
[[Category: p17]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:06:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:39 2008''

Revision as of 11:01, 21 February 2008


1hiw, resolution 2.3Å

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TRIMERIC HIV-1 MATRIX PROTEIN

Overview

The human immunodeficiency virus type 1 (HIV-1) matrix protein forms a structural shell associated with the inner viral membrane and performs other essential functions throughout the viral life cycle. The crystal structure of the HIV-1 matrix protein, determined at 2.3 angstrom resolution, reveals that individual matrix molecules are composed of five major helices capped by a three-stranded mixed beta-sheet. Unexpectedly, the protein assembles into a trimer in three different crystal lattices, burying 1880 angstrom2 of accessible surface area at the trimer interfaces. Trimerization appears to create a large, bipartite membrane binding surface in which exposed basic residues could cooperate with the N-terminal myristoyl groups to anchor the protein on the acidic inner membrane of the virus.

About this Structure

1HIW is a Single protein structure of sequence from Human immunodeficiency virus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly., Hill CP, Worthylake D, Bancroft DP, Christensen AM, Sundquist WI, Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3099-104. PMID:8610175

Page seeded by OCA on Thu Feb 21 13:01:39 2008

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