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rdf:type |
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lifeskim:mentions |
umls-concept:C0006675,
umls-concept:C0006784,
umls-concept:C0014442,
umls-concept:C0035820,
umls-concept:C0444626,
umls-concept:C0851285,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1514562,
umls-concept:C1706853,
umls-concept:C1879748,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1999216,
umls-concept:C2349209,
umls-concept:C2699488,
umls-concept:C2825311
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|
pubmed:issue |
7
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|
pubmed:dateCreated |
1997-8-13
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1072-8368
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pubmed:author |
pubmed-author:BosL PLP,
pubmed-author:CarsonMM,
pubmed-author:ChattopadhyayDD,
pubmed-author:DeLucasL JLJ,
pubmed-author:HatanakaMM,
pubmed-author:JinLL,
pubmed-author:MakiMM,
pubmed-author:NarayanaS VSV,
pubmed-author:TakanoEE,
pubmed-author:WannK TKT,
pubmed-author:YuenP WPW
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pubmed:issnType |
Print
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pubmed:volume |
4
|
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pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
539-47
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9228946-Acrylates,
pubmed-meshheading:9228946-Amino Acid Sequence,
pubmed-meshheading:9228946-Binding Sites,
pubmed-meshheading:9228946-Calcium,
pubmed-meshheading:9228946-Calpain,
pubmed-meshheading:9228946-Crystallography, X-Ray,
pubmed-meshheading:9228946-Cysteine Proteinase Inhibitors,
pubmed-meshheading:9228946-Dimerization,
pubmed-meshheading:9228946-Models, Molecular,
pubmed-meshheading:9228946-Molecular Sequence Data,
pubmed-meshheading:9228946-Protein Conformation,
pubmed-meshheading:9228946-Protein Folding,
pubmed-meshheading:9228946-Sequence Homology, Amino Acid
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pubmed:year |
1997
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pubmed:articleTitle |
Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding.
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|
pubmed:affiliation |
Center for Macromolecular Crystallography, University of Alabama at Birmingham 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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