| pubmed-article:14741217 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14741217 | lifeskim:mentions | umls-concept:C0668750 | lld:lifeskim |
| pubmed-article:14741217 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:14741217 | lifeskim:mentions | umls-concept:C1417205 | lld:lifeskim |
| pubmed-article:14741217 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:14741217 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:14741217 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:14741217 | lifeskim:mentions | umls-concept:C2348519 | lld:lifeskim |
| pubmed-article:14741217 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:14741217 | pubmed:dateCreated | 2004-1-26 | lld:pubmed |
| pubmed-article:14741217 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:abstractText | Membrane-type matrix metalloproteinases (MT-MMPs) have attracted strong attention, because four of them can activate a key player in the tumor scenario, proMMP-2/progelatinase A. In addition to this indirect effect on the cellular environment, these MT-MMPs degrade extracellular matrix proteins, and their overproduction is associated with tumor growth. We have solved the structure of the catalytic domain (cd) of MT3-MMP/MMP-16 in complex with the hydroxamic acid inhibitor batimastat. CdMT3-MMP exhibits a classical MMP-fold with similarity to MT1-MMP. Nevertheless, it also shows unique properties such as a modified MT-specific loop and a closed S1' specificity pocket, which might help to design specific inhibitors. Some MT-MMP-specific features, derived from the crystal structures of MT-1-MMP determined previously and MT3-MMP, and revealed in recent mutagenesis experiments, explain the impaired interaction of the MT-MMPs with TIMP-1. Docking experiments with proMMP-2 show some exposed loops including the MT-loop of cdMT3-MMP involved in the interaction with the proMMP-2 prodomain in the activation encounter complex. This model might help to understand the experimentally proven importance of the MT-loop for the activation of proMMP-2. | lld:pubmed |
| pubmed-article:14741217 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14741217 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14741217 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14741217 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:14741217 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:BodeWW | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:BraunMM | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:LangRR | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:NoelAA | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:MaskosKK | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:FrankenneFF | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:SounniN ENE | lld:pubmed |
| pubmed-article:14741217 | pubmed:author | pubmed-author:FoidartJ-MJM | lld:pubmed |
| pubmed-article:14741217 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14741217 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:14741217 | pubmed:volume | 336 | lld:pubmed |
| pubmed-article:14741217 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14741217 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14741217 | pubmed:pagination | 213-25 | lld:pubmed |
| pubmed-article:14741217 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:14741217 | pubmed:meshHeading | pubmed-meshheading:14741217... | lld:pubmed |
| pubmed-article:14741217 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14741217 | pubmed:articleTitle | Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features. | lld:pubmed |
| pubmed-article:14741217 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried-bei-munchen, Germany. | lld:pubmed |
| pubmed-article:14741217 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14741217 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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