1md7
From Proteopedia
(New page: 200px<br /> <applet load="1md7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1md7, resolution 3.20Å" /> '''Monomeric structure...) |
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| - | [[Image:1md7.gif|left|200px]]<br /> | + | [[Image:1md7.gif|left|200px]]<br /><applet load="1md7" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1md7, resolution 3.20Å" /> | caption="1md7, resolution 3.20Å" /> | ||
'''Monomeric structure of the zymogen of complement protease C1r'''<br /> | '''Monomeric structure of the zymogen of complement protease C1r'''<br /> | ||
==Overview== | ==Overview== | ||
| - | C1r is the serine protease (SP) that mediates autoactivation of C1, the | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MD7 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 NDG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41] Full crystallographic information is available from [http:// | + | 1MD7 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 <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arlaud, G | + | [[Category: Arlaud, G J.]] |
[[Category: Budayova-Spano, M.]] | [[Category: Budayova-Spano, M.]] | ||
[[Category: Fontecilla-Camps, J.]] | [[Category: Fontecilla-Camps, J.]] | ||
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[[Category: Lacroix, M.]] | [[Category: Lacroix, M.]] | ||
[[Category: Schmidt, M.]] | [[Category: Schmidt, M.]] | ||
| - | [[Category: Thielens, N | + | [[Category: Thielens, N M.]] |
[[Category: NDG]] | [[Category: NDG]] | ||
[[Category: activation]] | [[Category: activation]] | ||
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[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:02 2008'' |
Revision as of 11:54, 21 February 2008
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Monomeric structure of the zymogen of complement protease C1r
Contents |
Overview
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.
Disease
Known disease associated with this structure: C1r/C1s deficiency, combined OMIM:[216950]
About this Structure
1MD7 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Complement subcomponent C1r, with EC number 3.4.21.41 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
Page seeded by OCA on Thu Feb 21 13:54:02 2008
Categories: Complement subcomponent C1r | Homo sapiens | Single protein | Arlaud, G J. | Budayova-Spano, M. | Fontecilla-Camps, J. | Gaboriaud, C. | Grabarse, W. | Hillen, H. | Lacroix, M. | Schmidt, M. | Thielens, N M. | NDG | Activation | Complement | Innate immunity | Serine protease | Substrate specificity
