This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3c3r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3c3r.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3c3r.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3c3r| PDB=3c3r | SCENE= }}
{{STRUCTURE_3c3r| PDB=3c3r | SCENE= }}
-
'''ALIX BRO1 CHMP4C complex'''
+
===ALIX BRO1 CHMP4C complex===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18511562}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18511562 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18511562}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Transport]]
[[Category: Transport]]
[[Category: Transport protein]]
[[Category: Transport protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:48:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:59:15 2008''

Revision as of 10:59, 27 July 2008

Image:3c3r.png

Template:STRUCTURE 3c3r

ALIX BRO1 CHMP4C complex

Template:ABSTRACT PUBMED 18511562

About this Structure

3C3R is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from 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:18511562

Page seeded by OCA on Sun Jul 27 13:59:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3c3r"
Personal tools