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1NZ6

Crystal Structure of Auxilin J-Domain

Summary for 1NZ6
Entry DOI10.2210/pdb1nz6/pdb
DescriptorAuxilin (2 entities in total)
Functional Keywordsalpha helix, anti-parallel helix hairpin, protein binding
Biological sourceBos taurus (cattle)
Total number of polymer chains2
Total formula weight24048.62
Authors
Jiang, J.,Taylor, A.B.,Prasad, K.,Ishikawa-Brush, Y.,Hart, P.J.,Lafer, E.M.,Sousa, R. (deposition date: 2003-02-16, release date: 2003-04-22, Last modification date: 2024-10-30)
Primary citationJiang, J.,Taylor, A.B.,Prasad, K.,Ishikawa-Brush, Y.,Hart, P.J.,Lafer, E.M.,Sousa, R.
Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface.
Biochemistry, 42:5748-5753, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12741832
DOI: 10.1021/bi034270g
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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