Structural highlights
Function
[AUXI_BOVIN] Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
J-domains are widespread protein interaction modules involved in recruiting and stimulating the activity of Hsp70 family chaperones. We have determined the crystal structure of the J-domain of auxilin, a protein which is involved in uncoating clathrin-coated vesicles. Comparison to the known structures of J-domains from four other proteins reveals that the auxilin J-domain is the most divergent of all J-domain structures described to date. In addition to the canonical J-domain features described previously, the auxilin J-domain contains an extra N-terminal helix and a long loop inserted between helices I and II. The latter loop extends the positively charged surface which forms the Hsc70 binding site, and is shown by directed mutagenesis and surface plasmon resonance to contain side chains important for binding to Hsc70.
Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface.,Jiang J, Taylor AB, Prasad K, Ishikawa-Brush Y, Hart PJ, Lafer EM, Sousa R Biochemistry. 2003 May 20;42(19):5748-53. PMID:12741832[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fotin A, Cheng Y, Grigorieff N, Walz T, Harrison SC, Kirchhausen T. Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature. 2004 Dec 2;432(7017):649-53. Epub 2004 Oct 24. PMID:15502813 doi:10.1038/nature03078
- ↑ Jiang J, Taylor AB, Prasad K, Ishikawa-Brush Y, Hart PJ, Lafer EM, Sousa R. Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface. Biochemistry. 2003 May 20;42(19):5748-53. PMID:12741832 doi:10.1021/bi034270g
