|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5079
|
|
pubmed:dateCreated |
1992-12-1
|
|
pubmed:abstractText |
The smooth muscle myosin light chain kinase (smMLCK) catalytic core was modeled by using the crystallographic coordinates of the cyclic AMP-dependent protein kinase catalytic subunit (cAPK) and a bound pseudosubstrate inhibitor peptide, PKI(5-24). Despite only 30% identity in amino acid sequence, the MLCK sequence can be readily accommodated in this structure. With the exception of the short B-helix, all major elements of secondary structure in the core are very likely conserved. The active site of the modeled MLCK complements the known requirements for peptide substrate recognition. MLCK contains a pseudosubstrate sequence that overlaps the calmodulin binding domain and has been proposed to act as an intrasteric inhibitor and occupy the substrate binding site in the absence of Ca(2+)-calmodulin. The pseudosubstrate sequence can be modeled easily into the entire backbone of PKI(5-24). The results demonstrate that the intrasteric model for regulation of MLCK by intramolecular competitive inhibition is structurally plausible.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0036-8075
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
2
|
|
pubmed:volume |
258
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
130-5
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:1439761-Amino Acid Sequence,
pubmed-meshheading:1439761-Binding Sites,
pubmed-meshheading:1439761-Chromosome Mapping,
pubmed-meshheading:1439761-Crystallography,
pubmed-meshheading:1439761-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:1439761-Models, Molecular,
pubmed-meshheading:1439761-Molecular Sequence Data,
pubmed-meshheading:1439761-Molecular Structure,
pubmed-meshheading:1439761-Myosin-Light-Chain Kinase,
pubmed-meshheading:1439761-Oligopeptides,
pubmed-meshheading:1439761-Peptide Fragments,
pubmed-meshheading:1439761-Peptides,
pubmed-meshheading:1439761-Protein Binding,
pubmed-meshheading:1439761-Protein Kinases,
pubmed-meshheading:1439761-Sequence Alignment,
pubmed-meshheading:1439761-Sequence Homology
|
|
pubmed:year |
1992
|
|
pubmed:articleTitle |
Structural basis of the intrasteric regulation of myosin light chain kinases.
|
|
pubmed:affiliation |
Department of Chemistry, University of California San Diego, La Jolla 92093-0654.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
