| pubmed-article:1862343 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:1862343 | lifeskim:mentions | umls-concept:C0439596 | lld:lifeskim |
| pubmed-article:1862343 | pubmed:issue | 5018 | lld:pubmed |
| pubmed-article:1862343 | pubmed:dateCreated | 1991-8-30 | lld:pubmed |
| pubmed-article:1862343 | pubmed:abstractText | The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal structure of the complex is the basis of the analysis. The peptide inhibitor, derived from a naturally occurring heat-stable protein kinase inhibitor, contains an amphipathic helix that is followed by a turn and an extended conformation. The extended region occupies the cleft between the two lobes of the enzyme and contains a five-residue consensus recognition sequence common to all substrates and peptide inhibitors of the catalytic subunit. The helical portion of the peptide binds to a hydrophobic groove and conveys high affinity binding. Loops from both domains converge at the active site and contribute to a network of conserved residues at the sites of magnesium adenosine triphosphate binding and catalysis. Amino acids associated with peptide recognition, nonconserved, extend over a large surface area. | lld:pubmed |
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| pubmed-article:1862343 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1862343 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1862343 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1862343 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1862343 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:1862343 | pubmed:author | pubmed-author:TaylorS SSS | lld:pubmed |
| pubmed-article:1862343 | pubmed:author | pubmed-author:XuongN HNH | lld:pubmed |
| pubmed-article:1862343 | pubmed:author | pubmed-author:Ten EyckL FLF | lld:pubmed |
| pubmed-article:1862343 | pubmed:author | pubmed-author:KnightonD RDR | lld:pubmed |
| pubmed-article:1862343 | pubmed:author | pubmed-author:SowadskiJ MJM | lld:pubmed |
| pubmed-article:1862343 | pubmed:author | pubmed-author:ZhengJ HJH | lld:pubmed |
| pubmed-article:1862343 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1862343 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:1862343 | pubmed:volume | 253 | lld:pubmed |
| pubmed-article:1862343 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1862343 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1862343 | pubmed:pagination | 414-20 | lld:pubmed |
| pubmed-article:1862343 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:1862343 | pubmed:meshHeading | pubmed-meshheading:1862343-... | lld:pubmed |
| pubmed-article:1862343 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1862343 | pubmed:articleTitle | Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. | lld:pubmed |
| pubmed-article:1862343 | pubmed:affiliation | Department of Chemistry, University of California, San Diego, La Jolla 92093-0654. | lld:pubmed |
| pubmed-article:1862343 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1862343 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1862343 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1862343 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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