| pubmed-article:8605631 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8605631 | lifeskim:mentions | umls-concept:C0038410 | lld:lifeskim |
| pubmed-article:8605631 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:8605631 | lifeskim:mentions | umls-concept:C0220892 | lld:lifeskim |
| pubmed-article:8605631 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
| pubmed-article:8605631 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8605631 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:8605631 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:8605631 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8605631 | pubmed:dateCreated | 1996-5-21 | lld:pubmed |
| pubmed-article:8605631 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8605631 | pubmed:abstractText | All beta-lactam antibiotics exert their biological effects by interacting with a unique class of proteins, the penicillin-binding proteins (PBPs). These membrane proteins are involved in the biosynthesis of the murein or peptidoglycan, a mesh-like structure which completely surrounds the bacterial cell. Sequence similarities indicate that one domain of these proteins belongs to a large family of beta-lactam-recognizing proteins, which includes the active-site serine beta-lactamases. We here report the first three-dimensional crystal structure of a high molecular weight penicillin-binding protein, PBP2x of Streptococcus pneumoniae, at 3.5 A resolution. The molecule has three domains, the central domain being a transpeptidase, which is a suitable target for antibiotic development. | lld:pubmed |
| pubmed-article:8605631 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8605631 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8605631 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8605631 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8605631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8605631 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8605631 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8605631 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:8605631 | pubmed:author | pubmed-author:HakenbeckRR | lld:pubmed |
| pubmed-article:8605631 | pubmed:author | pubmed-author:DidebergOO | lld:pubmed |
| pubmed-article:8605631 | pubmed:author | pubmed-author:MoréPP | lld:pubmed |
| pubmed-article:8605631 | pubmed:author | pubmed-author:PétillotYY | lld:pubmed |
| pubmed-article:8605631 | pubmed:author | pubmed-author:ParesSS | lld:pubmed |
| pubmed-article:8605631 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8605631 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8605631 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8605631 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8605631 | pubmed:pagination | 284-9 | lld:pubmed |
| pubmed-article:8605631 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8605631 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8605631 | pubmed:articleTitle | X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. | lld:pubmed |
| pubmed-article:8605631 | pubmed:affiliation | Institut de Biologie Structurale, Laboratoire de Cristallographie Macromoléculaire, Grenoble, France. | lld:pubmed |
| pubmed-article:8605631 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8605631 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| literatureCitation:4154_860... | literatureCitation:pubmed | pubmed-article:8605631 | lld:drugbank |
| family:PF00905.17 | family:pubmed | pubmed-article:8605631 | lld:pfam |
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