2j0t

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[[Image:2j0t.jpg|left|200px]]<br /><applet load="2j0t" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2j0t.jpg|left|200px]]
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caption="2j0t, resolution 2.54&Aring;" />
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'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1'''<br />
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{{Structure
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|PDB= 2j0t |SIZE=350|CAPTION= <scene name='initialview01'>2j0t</scene>, resolution 2.54&Aring;
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|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+C'>AC1</scene>
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|LIGAND= <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/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2J0T 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=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/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0T OCA].
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2J0T 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=2J0T OCA].
==Reference==
==Reference==
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Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1., Iyer S, Wei S, Brew K, Acharya KR, J Biol Chem. 2007 Jan 5;282(1):364-71. Epub 2006 Oct 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17050530 17050530]
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Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1., Iyer S, Wei S, Brew K, Acharya KR, J Biol Chem. 2007 Jan 5;282(1):364-71. Epub 2006 Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17050530 17050530]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Interstitial collagenase]]
[[Category: Interstitial collagenase]]
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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 17:58:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:59 2008''

Revision as of 15:36, 20 March 2008

Image:2j0t.jpg


PDB ID 2j0t

Drag the structure with the mouse to rotate
, resolution 2.54Å
Sites:
Ligands: and
Activity: Interstitial collagenase, with EC number 3.4.24.7
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1


Contents

Overview

The mammalian collagenases are a subgroup of the matrix metalloproteinases (MMPs) that are uniquely able to cleave triple helical fibrillar collagens. Collagen breakdown is an essential part of extracellular matrix turnover in key physiological processes including morphogenesis and wound healing; however, unregulated collagenolysis is linked to important diseases such as arthritis and cancer. The tissue inhibitors of metalloproteinases (TIMPs) function in controlling the activity of MMPs, including collagenases. We report here the structure of a complex of the catalytic domain of fibroblast collagenase (MMP-1) with the N-terminal inhibitory domain of human TIMP-1 (N-TIMP-1) at 2.54 A resolution. Comparison with the previously reported structure of the TIMP-1/stromelysin-1 (MMP-3) complex shows that the mechanisms of inhibition of both MMPs are generally similar, yet there are significant differences in the protein-protein interfaces in the two complexes. Specifically, the loop between beta-strands A and B of TIMP-1 makes contact with MMP-3 but not with MMP-1, and there are marked differences in the roles of individual residues in the C-D connector of TIMP-1 in binding to the two MMPs. Structural rearrangements in the bound MMPs are also strikingly different. This is the first crystallographic structure that contains the truncated N-terminal domain of a TIMP, which shows only minor differences from the corresponding region of the full-length protein. Differences in the interactions in the two TIMP-1 complexes provide a structural explanation for the results of previous mutational studies and a basis for designing new N-TIMP-1 variants with restricted specificity.

Disease

Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353], Sorsby fundus dystrophy OMIM:[188826]

About this Structure

2J0T is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1., Iyer S, Wei S, Brew K, Acharya KR, J Biol Chem. 2007 Jan 5;282(1):364-71. Epub 2006 Oct 18. PMID:17050530

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