1ALW

INHIBITOR AND CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN

Summary for 1ALW

• Entry DOI: 10.2210/pdb1alw/pdb
• Descriptor: CALPAIN, CALCIUM ION, 3-(4-IODO-PHENYL)-2-MERCAPTO-PROPIONIC ACID, ... (4 entities in total)
• Functional Keywords: calcium binding, calmodulin like, domain of cystein protease
• Biological source: Sus scrofa (pig)
• Cellular location: Cytoplasm (By similarity): P04574
• Total number of polymer chains: 2
• Total formula weight: 40703.85

Authors

Narayana, S.V.L.,Lin, G. (deposition date: 1997-06-04, release date: 1998-06-10, Last modification date: 2024-04-03)

Primary citation

Lin, G.D.,Chattopadhyay, D.,Maki, M.,Wang, K.K.,Carson, M.,Jin, L.,Yuen, P.W.,Takano, E.,Hatanaka, M.,DeLucas, L.J.,Narayana, S.V.
Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding.
Nat.Struct.Biol., 4:539-547, 1997

PubMed Abstract: 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.

PubMed: 9228946
DOI: 10.1038/nsb0797-539

Experimental method

X-RAY DIFFRACTION (2.03 Å)