1hiw
From Proteopedia
(New page: 200px<br /> <applet load="1hiw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hiw, resolution 2.3Å" /> '''TRIMERIC HIV-1 MATRI...) |
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- | [[Image:1hiw.gif|left|200px]]<br /> | + | [[Image:1hiw.gif|left|200px]]<br /><applet load="1hiw" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1hiw" size=" | + | |
caption="1hiw, resolution 2.3Å" /> | caption="1hiw, resolution 2.3Å" /> | ||
'''TRIMERIC HIV-1 MATRIX PROTEIN'''<br /> | '''TRIMERIC HIV-1 MATRIX PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
- | The human immunodeficiency virus type 1 (HIV-1) matrix protein forms a | + | 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== | ||
- | 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:// | + | 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]] | ||
- | [[Category: Bancroft, D | + | [[Category: Bancroft, D P.]] |
- | [[Category: Christensen, A | + | [[Category: Christensen, A M.]] |
- | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
- | [[Category: Sundquist, W | + | [[Category: Sundquist, W I.]] |
[[Category: Worthylake, D.]] | [[Category: Worthylake, D.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: p17]] | [[Category: p17]] | ||
- | ''Page seeded by [http:// | + | ''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
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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