1elv
From Proteopedia
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|PDB= 1elv |SIZE=350|CAPTION= <scene name='initialview01'>1elv</scene>, resolution 1.7Å | |PDB= 1elv |SIZE=350|CAPTION= <scene name='initialview01'>1elv</scene>, resolution 1.7Å | ||
|SITE= <scene name='pdbsite=CAT:The+Catalytic+Triad+Is+HIS+A460+(57),+ASP+A514+(102),+SE+...'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:The+Catalytic+Triad+Is+HIS+A460+(57),+ASP+A514+(102),+SE+...'>CAT</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NES:2-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-ETHANESULFONIC+ACID'>NES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Complement_subcomponent_C1s Complement subcomponent C1s], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.42 3.4.21.42] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Complement_subcomponent_C1s Complement subcomponent C1s], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.42 3.4.21.42] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elv OCA], [http://www.ebi.ac.uk/pdbsum/1elv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elv RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
C1s is the highly specific modular serine protease that mediates the proteolytic activity of the C1 complex and thereby triggers activation of the complement cascade. The crystal structure of a catalytic fragment from human C1s comprising the second complement control protein (CCP2) module and the chymotrypsin-like serine protease (SP) domain has been determined and refined to 1.7 A resolution. In the areas surrounding the active site, the SP structure reveals a restricted access to subsidiary substrate binding sites that could be responsible for the narrow specificity of C1s. The ellipsoidal CCP2 module is oriented perpendicularly to the surface of the SP domain. This arrangement is maintained through a rigid module-domain interface involving intertwined proline- and tyrosine-rich polypeptide segments. The relative orientation of SP and CCP2 is consistent with the fact that the latter provides additional substrate recognition sites for the C4 substrate. This structure provides a first example of a CCP-SP assembly that is conserved in diverse extracellular proteins. Its implications in the activation mechanism of C1 are discussed. | C1s is the highly specific modular serine protease that mediates the proteolytic activity of the C1 complex and thereby triggers activation of the complement cascade. The crystal structure of a catalytic fragment from human C1s comprising the second complement control protein (CCP2) module and the chymotrypsin-like serine protease (SP) domain has been determined and refined to 1.7 A resolution. In the areas surrounding the active site, the SP structure reveals a restricted access to subsidiary substrate binding sites that could be responsible for the narrow specificity of C1s. The ellipsoidal CCP2 module is oriented perpendicularly to the surface of the SP domain. This arrangement is maintained through a rigid module-domain interface involving intertwined proline- and tyrosine-rich polypeptide segments. The relative orientation of SP and CCP2 is consistent with the fact that the latter provides additional substrate recognition sites for the C4 substrate. This structure provides a first example of a CCP-SP assembly that is conserved in diverse extracellular proteins. Its implications in the activation mechanism of C1 are discussed. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: C1r/C1s deficiency, combined OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120580 120580]], C1s deficiency, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120580 120580]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Gaboriaud, C.]] | [[Category: Gaboriaud, C.]] | ||
[[Category: Rossi, V.]] | [[Category: Rossi, V.]] | ||
| - | [[Category: NES]] | ||
| - | [[Category: SO4]] | ||
[[Category: ccp (or sushi or scr)module]] | [[Category: ccp (or sushi or scr)module]] | ||
[[Category: trypsin-like serin protease]] | [[Category: trypsin-like serin protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:05:12 2008'' |
Revision as of 17:05, 30 March 2008
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| , resolution 1.7Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Complement subcomponent C1s, with EC number 3.4.21.42 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE
Overview
C1s is the highly specific modular serine protease that mediates the proteolytic activity of the C1 complex and thereby triggers activation of the complement cascade. The crystal structure of a catalytic fragment from human C1s comprising the second complement control protein (CCP2) module and the chymotrypsin-like serine protease (SP) domain has been determined and refined to 1.7 A resolution. In the areas surrounding the active site, the SP structure reveals a restricted access to subsidiary substrate binding sites that could be responsible for the narrow specificity of C1s. The ellipsoidal CCP2 module is oriented perpendicularly to the surface of the SP domain. This arrangement is maintained through a rigid module-domain interface involving intertwined proline- and tyrosine-rich polypeptide segments. The relative orientation of SP and CCP2 is consistent with the fact that the latter provides additional substrate recognition sites for the C4 substrate. This structure provides a first example of a CCP-SP assembly that is conserved in diverse extracellular proteins. Its implications in the activation mechanism of C1 are discussed.
About this Structure
1ELV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle., Gaboriaud C, Rossi V, Bally I, Arlaud GJ, Fontecilla-Camps JC, EMBO J. 2000 Apr 17;19(8):1755-65. PMID:10775260
Page seeded by OCA on Sun Mar 30 20:05:12 2008
