2j83
From Proteopedia
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| - | [[Image:2j83.jpg|left|200px]]<br /><applet load="2j83" size=" | + | [[Image:2j83.jpg|left|200px]]<br /><applet load="2j83" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2j83, resolution 2.00Å" /> | caption="2j83, resolution 2.00Å" /> | ||
'''ULILYSIN METALLOPROTEASE IN COMPLEX WITH BATIMASTAT.'''<br /> | '''ULILYSIN METALLOPROTEASE IN COMPLEX WITH BATIMASTAT.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2J83 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans] with CA, ZN, BAT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2J83 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=BAT:'>BAT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J83 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pappalysin]] | [[Category: pappalysin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:42:43 2008'' |
Revision as of 08:42, 3 February 2008
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ULILYSIN METALLOPROTEASE IN COMPLEX WITH BATIMASTAT.
Overview
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.
About this Structure
2J83 is a Single protein structure of sequence from Methanosarcina acetivorans with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Feb 3 10:42:43 2008
Categories: Methanosarcina acetivorans | Single protein | Baumann, U. | Garcia-Castellanos, R. | Gomis-Ruth, F.X. | Marrero, A. | Sola, M. | Tallant, C. | BAT | CA | GOL | ZN | Batimastat | Bb-94 | Cancer | Hydrolase | Hydroxamate inhibitor | Hypothetical protein | Igf | Igfbp protease | Metalloprotease | Metzincin | Pappalysin
