This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1su3

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

X-ray structure of human proMMP-1: New insights into collagenase action

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1su3"

@@ Line 1: / Line 1: @@
-[[Image:1su3.gif|left|200px]]<br />
-<applet load="1su3" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1su3, resolution 2.20&Aring;" />
-'''X-ray structure of human proMMP-1: New insights into collagenase action'''<br />
-==Overview==
+==X-ray structure of human proMMP-1: New insights into collagenase action==
-Vertebrate collagenases, members of the matrix metalloproteinase (MMP), family, initiate interstitial fibrillar collagen breakdown. It is, essential in many biological processes, and unbalanced collagenolysis is, associated with diseases such as arthritis, cancer, atherosclerosis, aneurysm, and fibrosis. These metalloproteinases are secreted from the, cell as inactive precursors, procollagenases (proMMPs). To gain insights, into the structural basis of their activation mechanisms and collagen, binding, we have crystallized recombinant human proMMP-1 and determined, its structure to 2.2 A resolution. The catalytic metalloproteinase domain, and the C-terminal hemopexin (Hpx) domain show the classical MMP-fold, but, the structure has revealed new features in surface loops and domain, interaction. The prodomain is formed by a three-helix bundle and gives, insight into the stepwise activation mechanism of proMMP-1. The prodomain, interacts with the Hpx domain, which affects the position of the Hpx, domain relative to the catalytic domain. This interaction results in a, "closed" configuration of proMMP-1 in contrast to the "open" configuration, observed previously for the structure of active MMP-1. This is the first, evidence of mobility of the Hpx domain in relation to the catalytic, domain, providing an important clue toward the understanding of the, collagenase-collagen interaction and subsequent collagenolysis.
+<StructureSection load='1su3' size='340' side='right'caption='[[1su3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1su3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SU3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
+<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1su3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su3 OCA], [https://pdbe.org/1su3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1su3 RCSB], [https://www.ebi.ac.uk/pdbsum/1su3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1su3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MMP1_HUMAN MMP1_HUMAN] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.<ref>PMID:1645757</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/su/1su3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1su3 ConSurf].
+<div style="clear:both"></div>
-==Disease==
+==See Also==
-Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120353 120353]]
+*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-SU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, CL, NA, ZN, SO4 and EPE 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SU3 OCA].
+__TOC__
+</StructureSection>
-==Reference==
-X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding., Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K, J Biol Chem. 2005 Mar 11;280(10):9578-85. Epub 2004 Dec 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15611040 15611040]
 [[Category: Homo sapiens]]
-[[Category: Interstitial collagenase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Bode W]]
-[[Category: Bode, W.]]
+[[Category: Bourenkov G]]
-[[Category: Bourenkov, G.]]
+[[Category: Jozic D]]
-[[Category: Jozic, D.]]
+[[Category: Lim NH]]
-[[Category: Lim, N.H.]]
+[[Category: Maskos K]]
-[[Category: Maskos, K.]]
+[[Category: Nagase H]]
-[[Category: Nagase, H.]]
-[[Category: SPINE, Structural.Proteomics.in.Europe.]]
-[[Category: CA]]
-[[Category: CL]]
-[[Category: EPE]]
-[[Category: NA]]
-[[Category: SO4]]
-[[Category: ZN]]
-[[Category: exocite]]
-[[Category: hemopexin domain]]
-[[Category: prodomain]]
-[[Category: spine]]
-[[Category: structural genomics]]
-[[Category: structural proteomics in europe]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:17:41 2007''

1su3

From Proteopedia

Current revision

X-ray structure of human proMMP-1: New insights into collagenase action

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox