4ca1

Crystal structure of Siah1 at 1.58 A resolution.Crystal structure of Siah1 at 1.58 A resolution.

Structural highlights 4ca1 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , Related: 4c9z Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Siah1 is an E3 ubiquitin ligase that contributes to proteasome-mediated degradation of multiple targets in key cellular processes and which shows promise as a therapeutic target in oncology. Structures of a truncated Siah1 bound to peptide-based inhibitors have been reported. Here, new crystallization conditions have allowed the determination of a construct encompassing dual zinc-finger subdomains and substrate-binding domains at significantly higher resolution. Although the crystals appear isomorphous, two structures present distinct states in which the spatial orientation of one zinc-finger subdomain differs with respect to the rest of the dimeric protein. Such a difference, which is indicative of conformational freedom, infers potential biological relevance related to recognition of binding partners. The crystallization conditions and improved models of Siah1 may aid future studies investigating Siah1-ligand complexes. Two high-resolution structures of the human E3 ubiquitin ligase Siah1.,Rimsa V, Eadsforth TC, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1339-43., doi: 10.1107/S1744309113031448. Epub 2013 Nov 28. PMID:24316825 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ubiquitin protein ligase

spinqualitylabelsall models 4ca1, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image