1bqq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!--The below Structure Template creates the "Structure Box" on the page. It is automatically created and periodically refreshed. All changes to the Structu...)
Current revision (06:26, 30 October 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1bqq.gif|left|200px]]
 
-
<!--The below Structure Template creates the "Structure Box" on the page. It is automatically created and periodically refreshed. All changes to the Structure Template will be lost EXCEPT for changes in the PDB parameter (setting the PDB file loaded) or the SCENE parameter (setting the initial scene to display when the page is loaded). -->
+
==CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX==
-
<!-- STRUCTURE TEMPLATE BEGIN -->
+
<StructureSection load='1bqq' size='340' side='right'caption='[[1bqq]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
-
{{Structure
+
== Structural highlights ==
-
|PDB= 1bqq |SIZE=350|CAPTION= <scene name='initialview01'>1bqq</scene>, resolution 2.75&Aring;
+
<table><tr><td colspan='2'>[[1bqq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQQ FirstGlance]. <br>
-
|SITE=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
|ACTIVITY=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqq OCA], [https://pdbe.org/1bqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bqq RCSB], [https://www.ebi.ac.uk/pdbsum/1bqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bqq ProSAT]</span></td></tr>
-
|GENE=
+
</table>
-
|DOMAIN=
+
== Function ==
-
|RELATEDENTRY=
+
[https://www.uniprot.org/uniprot/MMP14_HUMAN MMP14_HUMAN] Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15.<ref>PMID:20837484</ref> <ref>PMID:22065321</ref>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqq OCA], [http://www.ebi.ac.uk/pdbsum/1bqq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bqq RCSB]</span>
+
== Evolutionary Conservation ==
-
}}
+
[[Image:Consurf_key_small.gif|200px|right]]
-
<!-- STRUCTURE TEMPLATE END -->
+
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/1bqq_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1bqq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
'''CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX'''
+
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<ref>PMID:9724659</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1bqq" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Matrix metalloproteinase|Matrix metalloproteinase]]
-
 
+
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
-
==About this Structure==
+
== References ==
-
1BQQ is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQQ OCA].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/9724659 9724659]
+
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Bode, W.]]
+
[[Category: Bode W]]
-
[[Category: Calvete, J J.]]
+
[[Category: Calvete JJ]]
-
[[Category: Fernandez-Catalan, C.]]
+
[[Category: Fernandez-Catalan C]]
-
[[Category: Huber, R.]]
+
[[Category: Huber R]]
-
[[Category: Lichte, A.]]
+
[[Category: Lichte A]]
-
[[Category: Maskos, K.]]
+
[[Category: Maskos K]]
-
[[Category: Tschesche, H.]]
+
[[Category: Tschesche H]]
-
[[Category: Turk, D.]]
+
[[Category: Turk D]]
-
[[Category: Crystal structure]]
+
-
[[Category: Matrix metalloproteinase]]
+
-
[[Category: Pro-gelatinase a activator]]
+
-
[[Category: Proteinase complex]]
+
-
[[Category: Tissue inhibitor of metalloproteinase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Apr 7 20:42:48 2008''
+

Current revision

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

PDB ID 1bqq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bqq"
Personal tools