| pubmed-article:1439761 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1439761 | lifeskim:mentions | umls-concept:C0027120 | lld:lifeskim |
| pubmed-article:1439761 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:1439761 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1439761 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:1439761 | pubmed:issue | 5079 | lld:pubmed |
| pubmed-article:1439761 | pubmed:dateCreated | 1992-12-1 | lld:pubmed |
| pubmed-article:1439761 | 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. | lld:pubmed |
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| pubmed-article:1439761 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1439761 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1439761 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1439761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1439761 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1439761 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1439761 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:1439761 | pubmed:author | pubmed-author:KempB EBE | lld:pubmed |
| pubmed-article:1439761 | pubmed:author | pubmed-author:MeansA RAR | lld:pubmed |
| pubmed-article:1439761 | pubmed:author | pubmed-author:TaylorS SSS | lld:pubmed |
| pubmed-article:1439761 | pubmed:author | pubmed-author:Ten EyckL FLF | lld:pubmed |
| pubmed-article:1439761 | pubmed:author | pubmed-author:KnightonD RDR | lld:pubmed |
| pubmed-article:1439761 | pubmed:author | pubmed-author:SowadskiJ MJM | lld:pubmed |
| pubmed-article:1439761 | pubmed:author | pubmed-author:PearsonR BRB | lld:pubmed |
| pubmed-article:1439761 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1439761 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:1439761 | pubmed:volume | 258 | lld:pubmed |
| pubmed-article:1439761 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1439761 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1439761 | pubmed:pagination | 130-5 | lld:pubmed |
| pubmed-article:1439761 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:1439761 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1439761 | pubmed:articleTitle | Structural basis of the intrasteric regulation of myosin light chain kinases. | lld:pubmed |
| pubmed-article:1439761 | pubmed:affiliation | Department of Chemistry, University of California San Diego, La Jolla 92093-0654. | lld:pubmed |
| pubmed-article:1439761 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1439761 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1439761 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1439761 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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