1gxd

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[[Image:1gxd.gif|left|200px]]<br /><applet load="1gxd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gxd.gif|left|200px]]
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caption="1gxd, resolution 3.10&Aring;" />
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'''PROMMP-2/TIMP-2 COMPLEX'''<br />
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{{Structure
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|PDB= 1gxd |SIZE=350|CAPTION= <scene name='initialview01'>1gxd</scene>, resolution 3.10&Aring;
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|SITE= <scene name='pdbsite=S4A:Ca+Binding+Site+For+Chain+B'>S4A</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24]
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|GENE=
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}}
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'''PROMMP-2/TIMP-2 COMPLEX'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GXD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] Known structural/functional Site: <scene name='pdbsite=S4A:Ca+Binding+Site+For+Chain+B'>S4A</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXD OCA].
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1GXD is a [[Protein complex]] structure of sequences 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=1GXD OCA].
==Reference==
==Reference==
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Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2., Morgunova E, Tuuttila A, Bergmann U, Tryggvason K, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7414-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12032297 12032297]
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Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2., Morgunova E, Tuuttila A, Bergmann U, Tryggvason K, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7414-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12032297 12032297]
[[Category: Gelatinase A]]
[[Category: Gelatinase A]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: collagen degradation]]
[[Category: collagen degradation]]
[[Category: extracellular matrix]]
[[Category: extracellular matrix]]
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[[Category: gelatinase a]]
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[[Category: gelatinase some]]
[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: matrix metalloproteinase 2]]
[[Category: matrix metalloproteinase 2]]
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[[Category: zymogen]]
[[Category: zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:29:18 2008''

Revision as of 09:29, 20 March 2008


PDB ID 1gxd

Drag the structure with the mouse to rotate
, resolution 3.10Å
Sites:
Ligands: , and
Activity: Gelatinase A, with EC number 3.4.24.24
Coordinates: save as pdb, mmCIF, xml



PROMMP-2/TIMP-2 COMPLEX


Contents

Overview

Matrix metalloproteinases (MMPs) are a family of multidomain enzymes involved in the physiological degradation of connective tissue, as well as in pathological states such as tumor invasion and arthritis. Apart from transcriptional regulation, MMPs are controlled by proenzyme activation and a class of specific tissue inhibitors of metalloproteinases (TIMPs) that bind to the catalytic site. TIMP-2 is a potent inhibitor of MMPs, but it has also been implicated in a unique cell surface activation mechanism of latent MMP-2/gelatinase A/type IV collagenase (proMMP-2), through its binding to the hemopexin domain of proMMP-2 on the one hand and to a membrane-type MMP activator on the other. The present crystal structure of the human proMMP-2/TIMP-2 complex reveals an interaction between the hemopexin domain of proMMP-2 and the C-terminal domain of TIMP-2, leaving the catalytic site of MMP-2 and the inhibitory site of TIMP-2 distant and spatially isolated. The interfacial contact of these two proteins is characterized by two distinct binding regions composed of alternating hydrophobic and hydrophilic interactions. This unique structure provides information for how specificity for noninhibitory MMP/TIMP complex formation is achieved.

Disease

Known diseases associated with this structure: Osteolysis, idiopathic, Saudi type OMIM:[120360], Winchester syndrome OMIM:[120360]

About this Structure

1GXD is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2., Morgunova E, Tuuttila A, Bergmann U, Tryggvason K, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7414-9. PMID:12032297

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