1gpz: Difference between revisions

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==Overview==
==Overview==
C1r is the modular serine protease (SP) that mediates autolytic activation, of C1, the macromolecular complex that triggers the classical pathway of, complement. The crystal structure of a mutated, proenzyme form of the, catalytic domain of human C1r, comprising the first and second complement, control protein modules (CCP1, CCP2) and the SP domain has been solved and, refined to 2.9 A resolution. The domain associates as a homodimer with an, elongated head-to-tail structure featuring a central opening and involving, interactions between the CCP1 module of one monomer and the SP domain of, its counterpart. Consequently, the catalytic site of one monomer and the, cleavage site of the other are located at opposite ends of the dimer. The, structure reveals unusual features in the SP domain ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11823416 (full description)]]
C1r is the modular serine protease (SP) that mediates autolytic activation, of C1, the macromolecular complex that triggers the classical pathway of, complement. The crystal structure of a mutated, proenzyme form of the, catalytic domain of human C1r, comprising the first and second complement, control protein modules (CCP1, CCP2) and the SP domain has been solved and, refined to 2.9 A resolution. The domain associates as a homodimer with an, elongated head-to-tail structure featuring a central opening and involving, interactions between the CCP1 module of one monomer and the SP domain of, its counterpart. Consequently, the catalytic site of one monomer and the, cleavage site of the other are located at opposite ends of the dimer. The, structure reveals unusual features in the SP domain and provides strong, support for the hypothesis that C1r activation in C1 is triggered by a, mechanical stress caused by target recognition that disrupts the CCP1-SP, interfaces and allows formation of transient states involving important, conformational changes.


==About this Structure==
==About this Structure==
1GPZ 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 NAG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: ASA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPZ OCA]].  
1GPZ 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: ASA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPZ OCA].  


==Reference==
==Reference==
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[[Category: serine protease]]
[[Category: serine protease]]


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