2r02: Difference between revisions
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[[Image:2r02.jpg|left|200px]] | [[Image:2r02.jpg|left|200px]] | ||
'''Crystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLTSL Late Domain''' | {{Structure | ||
|PDB= 2r02 |SIZE=350|CAPTION= <scene name='initialview01'>2r02</scene>, resolution 2.60Å | |||
|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]) | |||
}} | |||
'''Crystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLTSL Late Domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2R02 is a [ | 2R02 is a [[Protein complex]] structure of sequences 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=2R02 OCA]. | ||
==Reference== | ==Reference== | ||
Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV., Zhai Q, Fisher RD, Chung HY, Myszka DG, Sundquist WI, Hill CP, Nat Struct Mol Biol. 2008 Jan;15(1):43-9. Epub 2007 Dec 9. PMID:[http:// | Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV., Zhai Q, Fisher RD, Chung HY, Myszka DG, Sundquist WI, Hill CP, Nat Struct Mol Biol. 2008 Jan;15(1):43-9. Epub 2007 Dec 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18066081 18066081] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Hill, C P.]] | [[Category: Hill, C P.]] | ||
[[Category: Zhai, Q.]] | [[Category: Zhai, Q.]] | ||
[[Category: | [[Category: aid]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: capsid protein]] | [[Category: capsid protein]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
''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 18:31:18 2008'' |
Revision as of 19:31, 20 March 2008
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, resolution 2.60Å | |||||||
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Gene: | PDCD6IP, AIP1, ALIX, KIAA1375 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLTSL Late Domain
OverviewOverview
Retrovirus budding requires short peptide motifs (late domains) located within the viral Gag protein that function by recruiting cellular factors. The YPX(n)L late domains of HIV and other lentiviruses recruit the protein ALIX (also known as AIP1), which also functions in vesicle formation at the multivesicular body and in the abscission stage of cytokinesis. Here, we report the crystal structures of ALIX in complex with the YPX(n)L late domains from HIV-1 and EIAV. The two distinct late domains bind at the same site on the ALIX V domain but adopt different conformations that allow them to make equivalent contacts. Binding studies and functional assays verified the importance of key interface residues and revealed that binding affinities are tuned by context-dependent effects. These results reveal how YPX(n)L late domains recruit ALIX to facilitate virus budding and how ALIX can bind YPX(n)L sequences with both n = 1 and n = 3.
About this StructureAbout this Structure
2R02 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV., Zhai Q, Fisher RD, Chung HY, Myszka DG, Sundquist WI, Hill CP, Nat Struct Mol Biol. 2008 Jan;15(1):43-9. Epub 2007 Dec 9. PMID:18066081
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Protein complex
- Fisher, R D.
- Hill, C P.
- Zhai, Q.
- Aid
- Apoptosis
- Capsid protein
- Coiled-coil
- Cytoplasm
- Host-virus interaction
- Lipoprotein
- Membrane
- Metal-binding
- Myristate
- Nucleus
- Peptide
- Phosphorylation
- Polymorphism
- Protein transport
- Rna-binding
- Transport
- Viral nucleoprotein
- Virion
- Zinc
- Zinc-finger