1md7

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{{STRUCTURE_1md7| PDB=1md7 | SCENE= }}
{{STRUCTURE_1md7| PDB=1md7 | SCENE= }}
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'''Monomeric structure of the zymogen of complement protease C1r'''
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===Monomeric structure of the zymogen of complement protease C1r===
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==Overview==
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C1r is the serine protease (SP) that mediates autoactivation of C1, the complex that triggers the classical complement pathway. We have determined the crystal structure of two fragments from the human C1r catalytic domain, each encompassing the second complement control protein (CCP2) module and the SP domain. The wild-type species has an active structure, whereas the S637A mutant is a zymogen. The structures reveal a restricted hinge flexibility of the CCP2-SP interface, and both are characterized by the unique alpha-helical conformation of loop E. The zymogen activation domain exhibits high mobility, and the active structure shows a restricted access to most substrate binding subsites. Further implications relevant to the C1r self-activation process are derived from protein-protein interactions in the crystals.
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{{ABSTRACT_PUBMED_12429092}}
==About this Structure==
==About this Structure==
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[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Substrate specificity]]
[[Category: Substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:54:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:43:05 2008''

Revision as of 20:43, 2 July 2008

Image:1md7.png

Template:STRUCTURE 1md7

Monomeric structure of the zymogen of complement protease C1r

Template:ABSTRACT PUBMED 12429092

About this Structure

1MD7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism., Budayova-Spano M, Grabarse W, Thielens NM, Hillen H, Lacroix M, Schmidt M, Fontecilla-Camps JC, Arlaud GJ, Gaboriaud C, Structure. 2002 Nov;10(11):1509-19. PMID:12429092

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