2qy0
From Proteopedia
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| - | [[Image:2qy0.jpg|left|200px]] | + | [[Image:2qy0.jpg|left|200px]] |
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| - | '''Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts''' | + | {{Structure |
| + | |PDB= 2qy0 |SIZE=350|CAPTION= <scene name='initialview01'>2qy0</scene>, resolution 2.60Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+D+800'>AC1</scene>, <scene name='pdbsite=AC2:Gol+Binding+Site+For+Residue+B+801'>AC2</scene>, <scene name='pdbsite=AC3:Gol+Binding+Site+For+Residue+C+802'>AC3</scene>, <scene name='pdbsite=AC4:Gol+Binding+Site+For+Residue+D+803'>AC4</scene>, <scene name='pdbsite=AC5:Gol+Binding+Site+For+Residue+B+804'>AC5</scene>, <scene name='pdbsite=AC6:Gol+Binding+Site+For+Residue+C+805'>AC6</scene> and <scene name='pdbsite=AC7:Gol+Binding+Site+For+Residue+A+806'>AC7</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= C1R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
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| + | '''Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QY0 is a [ | + | 2QY0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QY0 OCA]. |
==Reference== | ==Reference== | ||
| - | Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r., Kardos J, Harmat V, Pallo A, Barabas O, Szilagyi K, Graf L, Naray-Szabo G, Goto Y, Zavodszky P, Gal P, Mol Immunol. 2008 Mar;45(6):1752-60. Epub 2007 Nov 9. PMID:[http:// | + | Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r., Kardos J, Harmat V, Pallo A, Barabas O, Szilagyi K, Graf L, Naray-Szabo G, Goto Y, Zavodszky P, Gal P, Mol Immunol. 2008 Mar;45(6):1752-60. Epub 2007 Nov 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17996945 17996945] |
[[Category: Complement subcomponent C1r]] | [[Category: Complement subcomponent C1r]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: sushi]] | [[Category: sushi]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:30:48 2008'' |
Revision as of 16:30, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Sites: | , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | C1R (Homo sapiens) | ||||||
| Activity: | Complement subcomponent C1r, with EC number 3.4.21.41 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts
Overview
C1r is a modular serine protease which is the autoactivating component of the C1 complex of the classical pathway of the complement system. We have determined the first crystal structure of the entire active catalytic region of human C1r. This fragment contains the C-terminal serine protease (SP) domain and the preceding two complement control protein (CCP) modules. The activated CCP1-CCP2-SP fragment makes up a dimer in a head-to-tail fashion similarly to the previously characterized zymogen. The present structure shows an increased number of stabilizing interactions. Moreover, in the crystal lattice there is an enzyme-product relationship between the C1r molecules of neighboring dimers. This enzyme-product complex exhibits the crucial S1-P1 salt bridge between Asp631 and Arg446 residues, and intermolecular interaction between the CCP2 module and the SP domain. Based on these novel structural information we propose a new split-and-reassembly model for the autoactivation of the C1r. This model is consistent with experimental results that have not been explained adequately by previous models. It allows autoactivation of C1r without large-scale, directed movement of C1q arms. The model is concordant with the stability of the C1 complex during activation of the next complement components.
About this Structure
2QY0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r., Kardos J, Harmat V, Pallo A, Barabas O, Szilagyi K, Graf L, Naray-Szabo G, Goto Y, Zavodszky P, Gal P, Mol Immunol. 2008 Mar;45(6):1752-60. Epub 2007 Nov 9. PMID:17996945
Page seeded by OCA on Thu Mar 20 18:30:48 2008
Categories: Complement subcomponent C1r | Homo sapiens | Protein complex | Barabas, O. | Gal, P. | Goto, Y. | Graf, L. | Harmat, V. | Kardos, J. | Naray-Szabo, G. | Pallo, A. | Szilagyi, K. | Zavodszky, P. | GOL | Beta barrel | Complement | Complement pathway | Egf-like domain | Glycoprotein | Hydrolase | Hydroxylation | Immune response | Innate immunity | Phosphorylation | Polymorphism | Serine protease | Sushi
