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1d2b

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[[Image:1d2b.jpg|left|200px]]<br /><applet load="1d2b" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d2b" />
 
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'''THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES'''<br />
 
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==Overview==
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==THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES==
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A high quality solution structure of the matrix metalloproteinase, inhibitory N-terminal domain of recombinant human tissue inhibitor of, metalloproteinases-1 (N-TIMP-1) has been determined. For the rigidly, packed residues, the average RMSD to the mean structure is 0. 57 A for the, backbone atoms and 1.00 A for all heavy atoms. Comparison of the solution, structure of free N-TIMP-1 with the crystal structure of TIMP-1 bound to, the catalytic domain of MMP-3 ( Gomis-R]uth et al., 1997 ) shows that the, structural core of the beta barrel flanked by helices is nearly unchanged, by the association with MMP-3, evident from a backbone RMSD of 1.15 A., However, clear differences in the conformation of the MMP-binding ridge of, free and MMP-bound TIMP-1 suggest induced fit throughout the ridge. The, MMP-dependent conformational changes in the ridge include a dramatic, bending of AB loop residues Glu28 through Leu34, moderate hinge bending of, the CD-loop about residues Ala65 and Cys70, and modest bending of the Cys1, through Pro6 segment. A large number of interresidue Nuclear Overhauser, enhancements (NOEs) augmented by stereospecific assignments, torsion, restraints, and dipolar couplings (an average of 18 non-trivial restraints, per residue) engender confidence in these structural inferences. A tight, cluster of three lysine residues and one arginine residue atop, beta-strands A and B, and identical among TIMP sequences, form the heart, of a highly conserved electropositive patch that may interact with anionic, components of the extracellular matrix.
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<StructureSection load='1d2b' size='340' side='right'caption='[[1d2b]]' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1d2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D2B FirstGlance]. <br>
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Known disease associated with this structure: Sorsby fundus dystrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188826 188826]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2b OCA], [https://pdbe.org/1d2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d2b RCSB], [https://www.ebi.ac.uk/pdbsum/1d2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d2b ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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1D2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2B OCA].
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== Function ==
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[https://www.uniprot.org/uniprot/TIMP1_HUMAN TIMP1_HUMAN] Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14.
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==Reference==
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== Evolutionary Conservation ==
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NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases., Wu B, Arumugam S, Gao G, Lee GI, Semenchenko V, Huang W, Brew K, Van Doren SR, J Mol Biol. 2000 Jan 14;295(2):257-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10623524 10623524]
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d2/1d2b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d2b ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arumugam, S.]]
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[[Category: Arumugam S]]
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[[Category: Brew, K.]]
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[[Category: Brew K]]
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[[Category: Doren, S.R.Van.]]
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[[Category: Semenchenko V]]
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[[Category: Semenchenko, V.]]
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[[Category: Van Doren SR]]
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[[Category: Wu, B.]]
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[[Category: Wu B]]
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[[Category: beta barrel]]
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[[Category: mmp inhibitor]]
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[[Category: ob-fold]]
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[[Category: protease inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:37:58 2008''
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Current revision

THE MMP-INHIBITORY, N-TERMINAL DOMAIN OF HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-1 (N-TIMP-1), SOLUTION NMR, 29 STRUCTURES

PDB ID 1d2b

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