2oew: Difference between revisions

Revision as of 19:17, 21 February 2008

Structure of ALIX/AIP1 Bro1 Domain

OverviewOverview

ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any residue; n = 1-3). Crystal structures reveal that human ALIX is composed of an N-terminal Bro1 domain and a central domain that is composed of two extended three-helix bundles that form elongated arms that fold back into a "V." The structures also reveal conformational flexibility in the arms that suggests that the V domain may act as a flexible hinge in response to ligand binding. YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding. ALIX therefore serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery.

About this StructureAbout this Structure

2OEW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding., Fisher RD, Chung HY, Zhai Q, Robinson H, Sundquist WI, Hill CP, Cell. 2007 Mar 9;128(5):841-52. PMID:17350572

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OCA

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 '''Structure of ALIX/AIP1 Bro1 Domain'''<br />
 ==Overview==
-ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and, EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any, residue; n = 1-3). Crystal structures reveal that human ALIX is composed, of an N-terminal Bro1 domain and a central domain that is composed of two, extended three-helix bundles that form elongated arms that fold back into, a "V." The structures also reveal conformational flexibility in the arms, that suggests that the V domain may act as a flexible hinge in response to, ligand binding. YPX(n)L late domains bind in a conserved hydrophobic, pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III, proteins bind a conserved hydrophobic patch on the Bro1 domain, and both, interactions are required for virus budding. ALIX therefore serves as a, flexible, extended scaffold that connects retroviral Gag proteins to, ESCRT-III and other cellular-budding machinery.
+ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any residue; n = 1-3). Crystal structures reveal that human ALIX is composed of an N-terminal Bro1 domain and a central domain that is composed of two extended three-helix bundles that form elongated arms that fold back into a "V." The structures also reveal conformational flexibility in the arms that suggests that the V domain may act as a flexible hinge in response to ligand binding. YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding. ALIX therefore serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery.
 ==About this Structure==
-OEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OEW OCA].
+OEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OEW OCA].
 ==Reference==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Fisher, R.D.]]
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-[[Category: Hill, C.P.]]
+[[Category: Hill, C P.]]
 [[Category: Robinson, H.]]
 [[Category: Zhai, Q.]]
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 [[Category: tpr]]
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