2r03
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Retrovirus budding requires short peptide motifs (late domains) located | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Fisher, R | + | [[Category: Fisher, R D.]] |
| - | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
[[Category: Zhai, Q.]] | [[Category: Zhai, Q.]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:44 2008'' |
Revision as of 16:43, 21 February 2008
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Crystal Structure of ALIX/AIP1 in complex with the YPDL Late Domain
Overview
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 Structure
2R03 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
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:18066081
Page seeded by OCA on Thu Feb 21 18:43:44 2008
Categories: Homo sapiens | Protein complex | Fisher, R D. | Hill, C P. | Zhai, Q. | Apoptosis | Capsid protein | Coiled-coil | Core protein | Cytoplasm | Host-virus interaction | Metal-binding | Peptide | Polymorphism | Protein transport | Transport | Virion | Zinc | Zinc-finger
