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2j83

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Revision as of 14:16, 7 February 2016

Ulilysin metalloprotease in complex with batimastat.

Structural highlights

2j83 is a 2 chain structure with sequence from Metac. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
NonStd Res:
Related:	2cki
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ULIL_METAC] Metalloprotease which in vitro specifically cleaves IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Shows a preference for substrates with an arginine in the P1' position, the first position downstream of the scissile bond.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human pappalysin-1 is a multi-domain metalloprotease engaged in the homeostasis of insulin-like growth factors and the founding member of the pappalysin family within the metzincin clan of metalloproteases. We have recently identified an archaeal relative, ulilysin, encompassing only the protease domain. It is a 262-residue active protease with a novel 3D structure with two subdomains separated by an active-site cleft. Despite negligible overall sequence similarity, noticeable similarity is found with other metzincin prototypes, adamalysins/ADAMs and matrix metalloproteinases. Ulilysin has been crystallised in a product complex with an arginine-valine dipeptide occupying the active-site S(1') and S(2') positions and in a complex with the broad-spectrum hydroxamic acid-based metalloprotease inhibitor, batimastat. This molecule inhibits mature ulilysin with an IC(50) value of 61 microM under the conditions assayed. The binding of batimastat to ulilysin evokes binding to vertebrate matrix metalloproteases but is much weaker. These data give insight into substrate specificity and mechanism of action and inhibition of the novel pappalysin family.

Substrate specificity of a metalloprotease of the pappalysin family revealed by an inhibitor and a product complex.,Garcia-Castellanos R, Tallant C, Marrero A, Sola M, Baumann U, Gomis-Ruth FX Arch Biochem Biophys. 2007 Jan 1;457(1):57-72. Epub 2006 Oct 24. PMID:17097044^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tallant C, Garcia-Castellanos R, Seco J, Baumann U, Gomis-Ruth FX. Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases. J Biol Chem. 2006 Jun 30;281(26):17920-8. Epub 2006 Apr 20. PMID:16627477 doi:10.1074/jbc.M600907200
↑ Garcia-Castellanos R, Tallant C, Marrero A, Sola M, Baumann U, Gomis-Ruth FX. Substrate specificity of a metalloprotease of the pappalysin family revealed by an inhibitor and a product complex. Arch Biochem Biophys. 2007 Jan 1;457(1):57-72. Epub 2006 Oct 24. PMID:17097044 doi:10.1016/j.abb.2006.10.004

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j83"

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cki|2cki]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j83 RCSB], [http://www.ebi.ac.uk/pdbsum/2j83 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j83 OCA], [http://pdbe.org/2j83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j83 RCSB], [http://www.ebi.ac.uk/pdbsum/2j83 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2j83 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2j83" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2j83

From Proteopedia

Revision as of 14:16, 7 February 2016

Ulilysin metalloprotease in complex with batimastat.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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