| pubmed-article:15388923 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15388923 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:15388923 | lifeskim:mentions | umls-concept:C0243795 | lld:lifeskim |
| pubmed-article:15388923 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:15388923 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:15388923 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15388923 | lifeskim:mentions | umls-concept:C0384979 | lld:lifeskim |
| pubmed-article:15388923 | pubmed:issue | Pt 10 | lld:pubmed |
| pubmed-article:15388923 | pubmed:dateCreated | 2004-9-24 | lld:pubmed |
| pubmed-article:15388923 | pubmed:abstractText | Aminopeptidase P (APPro) is a metalloprotease whose active site includes a dinuclear manganese(II) cluster. The enzyme cleaves the N-terminal residue from a polypeptide when the second residue is proline. A complex of Escherichia coli APPro (EcAPPro) with an inhibitor, apstatin [N-(2S,3R)-3-amino-2-hydroxy-4-phenyl-butanoyl-L-prolyl-L-prolyl-L-alaninamide], has been crystallized. Apstatin binds to the active site of EcAPPro with its N-terminal amino group coordinated to one of the two Mn(II) atoms at the metal centre. The apstatin hydroxyl group replaces a hydroxide ion which bridges the two metal atoms in the native enzyme. The first proline residue of apstatin lies in a small hydrophobic cleft. The structure of the apstatin-EcAPPro complex has been refined at 2.3 A resolution with residuals R = 0.179 and R(free) = 0.204. The structure of the complex illustrates how apstatin inhibits APPro and suggests how substrates may bind to the enzyme, but the basis of the proline-specificity remains elusive. | lld:pubmed |
| pubmed-article:15388923 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15388923 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15388923 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15388923 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15388923 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:15388923 | pubmed:author | pubmed-author:GussJ... | lld:pubmed |
| pubmed-article:15388923 | pubmed:author | pubmed-author:SimmonsWillia... | lld:pubmed |
| pubmed-article:15388923 | pubmed:author | pubmed-author:MaherMegan... | lld:pubmed |
| pubmed-article:15388923 | pubmed:author | pubmed-author:FreemanHans... | lld:pubmed |
| pubmed-article:15388923 | pubmed:author | pubmed-author:GrahamStephen... | lld:pubmed |
| pubmed-article:15388923 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15388923 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:15388923 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15388923 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15388923 | pubmed:pagination | 1770-9 | lld:pubmed |
| pubmed-article:15388923 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
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| pubmed-article:15388923 | pubmed:meshHeading | pubmed-meshheading:15388923... | lld:pubmed |
| pubmed-article:15388923 | pubmed:meshHeading | pubmed-meshheading:15388923... | lld:pubmed |
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| pubmed-article:15388923 | pubmed:meshHeading | pubmed-meshheading:15388923... | lld:pubmed |
| pubmed-article:15388923 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15388923 | pubmed:articleTitle | Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin. | lld:pubmed |
| pubmed-article:15388923 | pubmed:affiliation | School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia. | lld:pubmed |
| pubmed-article:15388923 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15388923 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947385 | entrezgene:pubmed | pubmed-article:15388923 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15388923 | lld:entrezgene |
