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000094201 0247_ $$2pmc$$apmc:PMC2676012
000094201 0247_ $$2doi$$a10.1074/jbc.M809627200
000094201 0247_ $$2ISSN$$a1083-351X
000094201 0247_ $$2ISSN$$a0021-9258
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000094201 037__ $$aPHPPUBDB-11922
000094201 041__ $$aeng
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000094201 1001_ $$aBertini, I.
000094201 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000094201 245__ $$aInterdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)
000094201 260__ $$aBethesda, Md.$$bSoc.$$c2009
000094201 300__ $$a12821-12828
000094201 3367_ $$00$$2EndNote$$aJournal Article
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000094201 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000094201 440_0 $$0PERI:(DE-600)1474604-9$$aJ. Biol. Chem.$$v284$$x0021-9258
000094201 500__ $$3Converted on 2013-05-30 14:57
000094201 500__ $$3Converted on 2013-06-21 19:21
000094201 520__ $$aThe presence of extensive reciprocal conformational freedom between the catalytic and the hemopexin-like domains of full-length matrix metalloproteinase-1 (MMP-1) is demonstrated by NMR and small angle x-ray scattering experiments. This finding is discussed in relation to the essentiality of the hemopexin-like domain for the collagenolytic activity of MMP-1. The conformational freedom experienced by the present system, having the shortest linker between the two domains, when compared with similar findings on MMP-12 and MMP-9 having longer and the longest linker within the family, respectively, suggests this type of conformational freedom to be a general property of all MMPs.
000094201 536__ $$0G:(DE-H253)POF1-No-Ref-20130405$$aFS Beamline without reference (POF1-550)$$cPOF1-550$$fPOF I$$x0
000094201 588__ $$aDataset connected to Pubmed
000094201 650_2 $$2MeSH$$aCatalysis
000094201 650_2 $$2MeSH$$aCrystallography, X-Ray
000094201 650_2 $$2MeSH$$aHeme
000094201 650_2 $$2MeSH$$aHumans
000094201 650_2 $$2MeSH$$aMatrix Metalloproteinase 1: chemistry
000094201 650_2 $$2MeSH$$aMatrix Metalloproteinase 1: metabolism
000094201 650_2 $$2MeSH$$aMatrix Metalloproteinase 12: chemistry
000094201 650_2 $$2MeSH$$aMatrix Metalloproteinase 9: chemistry
000094201 650_2 $$2MeSH$$aModels, Molecular
000094201 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000094201 650_2 $$2MeSH$$aPliability
000094201 650_2 $$2MeSH$$aProtein Conformation
000094201 650_2 $$2MeSH$$aProtein Structure, Tertiary
000094201 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000094201 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000094201 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000094201 650_7 $$014875-96-8$$2NLM Chemicals$$aHeme
000094201 650_7 $$0EC 3.4.24.35$$2NLM Chemicals$$aMatrix Metalloproteinase 9
000094201 650_7 $$0EC 3.4.24.65$$2NLM Chemicals$$aMatrix Metalloproteinase 12
000094201 650_7 $$0EC 3.4.24.7$$2NLM Chemicals$$aMatrix Metalloproteinase 1
000094201 693__ $$0EXP:(DE-H253)Unknown-BL-20150101$$6EXP:(DE-H253)Unknown-BL-20150101$$fUnknown DESY Beamline$$x0
000094201 7001_ $$aFragai, M.
000094201 7001_ $$aLuchinat, C.
000094201 7001_ $$aMelikian, M.
000094201 7001_ $$aMylonas, E.
000094201 7001_ $$aSarti, N.
000094201 7001_ $$aSvergun, D. I.
000094201 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M809627200$$gVol. 284, p. 12821-12828$$p12821-12828$$q284<12821-12828$$tThe @journal of biological chemistry$$v284$$x0021-9258$$y2009
000094201 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2676012
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000094201 9141_ $$a(c) 2010 by American Society for Biochemistry and Molecular Biology. No copyright permission for full text.$$y2009
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000094201 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
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