1alv
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CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN
OverviewOverview
The three dimensional structure of calcium-bound domain VI of porcine, calpain has been determined to 1.9 A resolution. The crystal structure, reveals five EF-hands, one more than previously suggested. There are two, EF-hand pairs, one pair (EF1-EF2) displays an 'open' conformation and the, other (EF3-EF4) a 'closed' conformation. Unusually, a calcium atom is, found at the C-terminal end of the calcium binding loop of EF4. With two, additional residues in the calcium binding loop, the fifth EF-hand (EF5), is in a 'closed' conformation. EF5 pairs up with the corresponding fifth, EF-hand of a non-crystallographically related molecule. Considering the, EF5's role in a homodimer formation of domain VI, we suggest a model for, the assembly of heterodimeric calpain. The crystal structure of a Ca2+, bound domain VI-inhibitor (PD150606) complex has been refined to 2.1 A, resolution. A possible mode for calpain inhibition is discussed.
About this StructureAbout this Structure
1ALV is a Single protein structure of sequence from Sus scrofa with CA as ligand. Active as Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding., Lin GD, Chattopadhyay D, Maki M, Wang KK, Carson M, Jin L, Yuen PW, Takano E, Hatanaka M, DeLucas LJ, Narayana SV, Nat Struct Biol. 1997 Jul;4(7):539-47. PMID:9228946
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