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| - | [[Image:2cki.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2cki| PDB=2cki | SCENE= }} | | {{STRUCTURE_2cki| PDB=2cki | SCENE= }} |
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| - | '''STRUCTURE OF ULILYSIN, A MEMBER OF THE PAPPALYSIN FAMILY OF METZINCIN METALLOENDOPEPTIDASES.'''
| + | ===STRUCTURE OF ULILYSIN, A MEMBER OF THE PAPPALYSIN FAMILY OF METZINCIN METALLOENDOPEPTIDASES.=== |
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| - | ==Overview==
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| - | The metzincin clan encompasses several families of zinc-dependent metalloproteases with proven function both in physiology and pathology. They act either as broad spectrum protein degraders or as sheddases, operating through limited proteolysis. Among the structurally uncharacterized metzincin families are the pappalysins, of which the most thoroughly studied member is human pregnancy-associated plasma protein A (PAPP-A), a heavily glycosylated 170-kDa multidomain protein specifically cleaving insulin-like growth factor (IGF)-binding proteins (IGFBPs). Proulilysin is a 38-kDa archaeal protein that shares sequence similarity with PAPP-A but encompasses only the pro-domain and the catalytic domain. It undergoes calcium-mediated autolytic activation, and the mature protein adopts a three-dimensional structure with two subdomains separated by an active site cleft containing the catalytic zinc ion. This structure is reminiscent of human members of the adamalysin/ADAMs (a disintegrin and a metalloprotease) family of metzincins. A bound dipeptide yields information on the substrate specificity of ulilysin, which specifically hydrolyzes IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Accordingly, ulilysin has higher proteolytic efficiency and a broader substrate specificity than human PAPP-A. The structure of ulilysin represents a prototype for the catalytic domain of pappalysins. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16627477}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16627477 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16627477}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Metzincin]] | | [[Category: Metzincin]] |
| | [[Category: Pappalysin]] | | [[Category: Pappalysin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:21:31 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:36:20 2008'' |
Revision as of 22:36, 27 July 2008
Template:STRUCTURE 2cki
STRUCTURE OF ULILYSIN, A MEMBER OF THE PAPPALYSIN FAMILY OF METZINCIN METALLOENDOPEPTIDASES.
Template:ABSTRACT PUBMED 16627477
About this Structure
2CKI is a Single protein structure of sequence from Methanosarcina acetivorans. Full crystallographic information is available from OCA.
Reference
Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases., Tallant C, Garcia-Castellanos R, Seco J, Baumann U, Gomis-Ruth FX, J Biol Chem. 2006 Jun 30;281(26):17920-8. Epub 2006 Apr 20. PMID:16627477
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