| pubmed-article:14978285 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14978285 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:14978285 | lifeskim:mentions | umls-concept:C0015982 | lld:lifeskim |
| pubmed-article:14978285 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:14978285 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:14978285 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:14978285 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
| pubmed-article:14978285 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:14978285 | pubmed:dateCreated | 2004-3-3 | lld:pubmed |
| pubmed-article:14978285 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14978285 | pubmed:abstractText | Nonsubstrate interactions of thrombin with fibrin play an important role in modulating its procoagulant activity. To establish the structural basis for these interactions, we crystallized d-Phe-Pro-Arg-chloromethyl ketone-inhibited human thrombin in complex with a fragment, E(ht), corresponding to the central region of human fibrin, and solved its structure at 3.65-A resolution. The structure revealed that the complex consists of two thrombin molecules bound to opposite sides of the central part of E(ht) in a way that seems to provide proper orientation of their catalytic triads for cleavage of fibrinogen fibrinopeptides. As expected, binding occurs through thrombin's anion-binding exosite I. However, only part of it is involved in forming an interface with the complementary negatively charged surface of E(ht). Among residues constituting the interface, Phe-34, Ser-36A, Leu-65, Tyr-76, Arg-77A, Ile-82, and Lys-110 of thrombin and the A alpha chain Trp-33, Phe-35, Asp-38, Glu-39, the B beta chain Ala-68 and Asp-69, and the gamma chain Asp-27 and Ser-30 of E(ht) form a net of polar contacts surrounding a well defined hydrophobic interior. Thus, despite the highly charged nature of the interacting surfaces, hydrophobic contacts make a substantial contribution to the interaction. | lld:pubmed |
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| pubmed-article:14978285 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14978285 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14978285 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14978285 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14978285 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14978285 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:14978285 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:14978285 | pubmed:author | pubmed-author:GillilandGary... | lld:pubmed |
| pubmed-article:14978285 | pubmed:author | pubmed-author:MedvedLeonidL | lld:pubmed |
| pubmed-article:14978285 | pubmed:author | pubmed-author:MosessonMicha... | lld:pubmed |
| pubmed-article:14978285 | pubmed:author | pubmed-author:HernandezIren... | lld:pubmed |
| pubmed-article:14978285 | pubmed:author | pubmed-author:PechikIgorI | lld:pubmed |
| pubmed-article:14978285 | pubmed:author | pubmed-author:MadrazoJoelJ | lld:pubmed |
| pubmed-article:14978285 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14978285 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:14978285 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:14978285 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14978285 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14978285 | pubmed:pagination | 2718-23 | lld:pubmed |
| pubmed-article:14978285 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:14978285 | pubmed:meshHeading | pubmed-meshheading:14978285... | lld:pubmed |
| pubmed-article:14978285 | pubmed:meshHeading | pubmed-meshheading:14978285... | lld:pubmed |
| pubmed-article:14978285 | pubmed:meshHeading | pubmed-meshheading:14978285... | lld:pubmed |
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| pubmed-article:14978285 | pubmed:meshHeading | pubmed-meshheading:14978285... | lld:pubmed |
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| pubmed-article:14978285 | pubmed:meshHeading | pubmed-meshheading:14978285... | lld:pubmed |
| pubmed-article:14978285 | pubmed:meshHeading | pubmed-meshheading:14978285... | lld:pubmed |
| pubmed-article:14978285 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14978285 | pubmed:articleTitle | Crystal structure of the complex between thrombin and the central "E" region of fibrin. | lld:pubmed |
| pubmed-article:14978285 | pubmed:affiliation | Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855, USA. medvedL@usa.redcross.org | lld:pubmed |
| pubmed-article:14978285 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14978285 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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