2oex: Difference between revisions
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[[Image:2oex.gif|left|200px]] | [[Image:2oex.gif|left|200px]] | ||
'''Structure of ALIX/AIP1 V Domain''' | {{Structure | ||
|PDB= 2oex |SIZE=350|CAPTION= <scene name='initialview01'>2oex</scene>, resolution 2.58Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= PDCD6IP, AIP1, ALIX, KIAA1375 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Structure of ALIX/AIP1 V Domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OEX is a [ | 2OEX is a [[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=2OEX OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17350572 17350572] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:58:48 2008'' | ||
Revision as of 18:58, 20 March 2008
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| , resolution 2.58Å | |||||||
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| Gene: | PDCD6IP, AIP1, ALIX, KIAA1375 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of ALIX/AIP1 V 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
2OEX 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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