1y9v

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

HOMOLOGY-BASED MODEL OF A HOMO-DIMER OF HUMAN CALPAIN 3 (P94) PENTA-EF HAND DOMAIN (DOMAIN IV)HOMOLOGY-BASED MODEL OF A HOMO-DIMER OF HUMAN CALPAIN 3 (P94) PENTA-EF HAND DOMAIN (DOMAIN IV)

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Calpains 1 and 2 are heterodimeric proteases in which large (relative molecular mass M(r) 80000) and small (M(r) 28000) subunits are linked through their respective PEF (penta-EF-hand) domains. The skeletal muscle-specific calpain 3 is believed not to form a heterodimer with the small subunit but might homodimerize through its PEF domain. Size-exclusion chromatography and analytical ultracentrifugation of the recombinant PEF domain of calpain 3 show that it forms a stable homodimer that does not dissociate on dilution. Molecular modelling suggests that there would be no barriers to the dimerization of the whole enzyme through the PEF domains. This orientation would place the catalytic centres at opposite ends of the dimer. Homodimerization of calpain 3 penta-EF-hand domain.,Ravulapalli R, Diaz BG, Campbell RL, Davies PL Biochem J. 2005 Jun 1;388(Pt 2):585-91. PMID:15660530 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1y9v Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image