1buv

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(New page: 200px<br /> <applet load="1buv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1buv, resolution 2.75&Aring;" /> '''CRYSTAL STRUCTURE O...)
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'''CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX'''<br />
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==About this Structure==
==About this Structure==
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1BUV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Membrane-type_matrix_metalloproteinase-1 Membrane-type matrix metalloproteinase-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.80 3.4.24.80] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BUV OCA].
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1BUV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Membrane-type_matrix_metalloproteinase-1 Membrane-type matrix metalloproteinase-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.80 3.4.24.80] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUV OCA].
==Reference==
==Reference==
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[[Category: tissue inhibitor of metalloproteinases]]
[[Category: tissue inhibitor of metalloproteinases]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:14:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:33:30 2008''

Revision as of 13:33, 15 February 2008


1buv, resolution 2.75Å

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CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX

Overview

The proteolytic activity of matrix metalloproteinases (MMPs) towards, extracellular matrix components is held in check by the tissue inhibitors, of metalloproteinases (TIMPs). The binary complex of TIMP-2 and, membrane-type-1 MMP (MT1-MMP) forms a cell surface located 'receptor', involved in pro-MMP-2 activation. We have solved the 2.75 A crystal, structure of the complex between the catalytic domain of human MT1-MMP, (cdMT1-MMP) and bovine TIMP-2. In comparison with our previously, determined MMP-3-TIMP-1 complex, both proteins are considerably tilted to, one another and show new features. CdMT1-MMP, apart from exhibiting the, classical MMP fold, displays two large insertions remote from the, active-site cleft that might be important for interaction with, macromolecular substrates. The TIMP-2 polypeptide chain, as in TIMP-1, folds into a continuous wedge; the A-B edge loop is much more elongated, and tilted, however, wrapping around the S-loop and the beta-sheet rim of, the MT1-MMP. In addition, both C-terminal edge loops make more, interactions with the target enzyme. The C-terminal acidic tail of TIMP-2, is disordered but might adopt a defined structure upon binding to, pro-MMP-2; the Ser2 side-chain of TIMP-2 extends into the voluminous S1', specificity pocket of cdMT1-MMP, with its Ogamma pointing towards the, carboxylate of the catalytic Glu240. The lower affinity of TIMP-1 for, MT1-MMP compared with TIMP-2 might be explained by a reduced number of, favourable interactions.

About this Structure

1BUV is a Protein complex structure of sequences from Bos taurus and Homo sapiens with and as ligands. Active as Membrane-type matrix metalloproteinase-1, with EC number 3.4.24.80 Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor., Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K, EMBO J. 1998 Sep 1;17(17):5238-48. PMID:9724659

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