3c3q: Difference between revisions
New page: '''Unreleased structure''' The entry 3c3q is ON HOLD until Paper Publication Authors: McCullough, J.B., Fisher, R.D., Whitby, F.G., Sundquist, W.I., Hill, C.P. Description: ALIX Bro1-d... |
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{{STRUCTURE_3c3q| PDB=3c3q | SCENE= }} | |||
'''ALIX Bro1-domain:CHMIP4B co-crystal structure''' | |||
==Overview== | |||
The ESCRT pathway facilitates membrane fission events during enveloped virus budding, multivesicular body formation, and cytokinesis. To promote HIV budding and cytokinesis, the ALIX protein must bind and recruit CHMP4 subunits of the ESCRT-III complex, which in turn participate in essential membrane remodeling functions. Here, we report that the Bro1 domain of ALIX binds specifically to C-terminal residues of the human CHMP4 proteins (CHMP4A-C). Crystal structures of the complexes reveal that the CHMP4 C-terminal peptides form amphipathic helices that bind across the conserved concave surface of ALIX(Bro1). ALIX-dependent HIV-1 budding is blocked by mutations in exposed ALIX(Bro1) residues that help contribute to the binding sites for three essential hydrophobic residues that are displayed on one side of the CHMP4 recognition helix (M/L/IxxLxxW). The homologous CHMP1-3 classes of ESCRT-III proteins also have C-terminal amphipathic helices, but, in those cases, the three hydrophobic residues are arrayed with L/I/MxxxLxxL spacing. Thus, the distinct patterns of hydrophobic residues provide a "code" that allows the different ESCRT-III subunits to bind different ESCRT pathway partners, with CHMP1-3 proteins binding MIT domain-containing proteins, such as VPS4 and Vta1/LIP5, and CHMP4 proteins binding Bro1 domain-containing proteins, such as ALIX. | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 | ==About this Structure== | ||
3C3Q 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=3C3Q OCA]. | |||
==Reference== | |||
ALIX-CHMP4 interactions in the human ESCRT pathway., McCullough J, Fisher RD, Whitby FG, Sundquist WI, Hill CP, Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7687-91. Epub 2008 May 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18511562 18511562] | |||
[[Category: Homo sapiens]] | |||
[[Category: Protein complex]] | |||
[[Category: Fisher, R D.]] | |||
[[Category: Hill, C P.]] | |||
[[Category: McCullough, J B.]] | |||
[[Category: Sundquist, W I.]] | |||
[[Category: Whitby, F G.]] | |||
[[Category: Alix chmp4b bro1 amphipathic-helix]] | |||
[[Category: Apoptosis]] | |||
[[Category: Cataract]] | |||
[[Category: Coiled coil]] | |||
[[Category: Cytoplasm]] | |||
[[Category: Disease mutation]] | |||
[[Category: Host-virus interaction]] | |||
[[Category: Polymorphism]] | |||
[[Category: Protein transport]] | |||
[[Category: Transport]] | |||
[[Category: Transport protein]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:48:02 2008'' | |||
Revision as of 10:48, 11 June 2008
ALIX Bro1-domain:CHMIP4B co-crystal structure
OverviewOverview
The ESCRT pathway facilitates membrane fission events during enveloped virus budding, multivesicular body formation, and cytokinesis. To promote HIV budding and cytokinesis, the ALIX protein must bind and recruit CHMP4 subunits of the ESCRT-III complex, which in turn participate in essential membrane remodeling functions. Here, we report that the Bro1 domain of ALIX binds specifically to C-terminal residues of the human CHMP4 proteins (CHMP4A-C). Crystal structures of the complexes reveal that the CHMP4 C-terminal peptides form amphipathic helices that bind across the conserved concave surface of ALIX(Bro1). ALIX-dependent HIV-1 budding is blocked by mutations in exposed ALIX(Bro1) residues that help contribute to the binding sites for three essential hydrophobic residues that are displayed on one side of the CHMP4 recognition helix (M/L/IxxLxxW). The homologous CHMP1-3 classes of ESCRT-III proteins also have C-terminal amphipathic helices, but, in those cases, the three hydrophobic residues are arrayed with L/I/MxxxLxxL spacing. Thus, the distinct patterns of hydrophobic residues provide a "code" that allows the different ESCRT-III subunits to bind different ESCRT pathway partners, with CHMP1-3 proteins binding MIT domain-containing proteins, such as VPS4 and Vta1/LIP5, and CHMP4 proteins binding Bro1 domain-containing proteins, such as ALIX.
About this StructureAbout this Structure
3C3Q is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
ALIX-CHMP4 interactions in the human ESCRT pathway., McCullough J, Fisher RD, Whitby FG, Sundquist WI, Hill CP, Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7687-91. Epub 2008 May 29. PMID:18511562 Page seeded by OCA on Wed Jun 11 10:48:02 2008