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1nzi

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Revision as of 07:34, 7 February 2018

Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s

Structural highlights

1nzi is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	C1S (HUMAN)
Activity:	Complement subcomponent C1s, with EC number 3.4.21.42
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[C1S_HUMAN] Defects in C1S are the cause of complement component C1s deficiency (C1SD) [MIM:613783]. A rare defect resulting in C1 deficiency and impaired activation of the complement classical pathway. C1 deficiency generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis.

Function

[C1S_HUMAN] C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

C1, the complex that triggers the classical pathway of complement, is assembled from two modular proteases C1r and C1s and a recognition protein C1q. The N-terminal CUB1-EGF segments of C1r and C1s are key elements of the C1 architecture, because they mediate both Ca2+-dependent C1r-C1s association and interaction with C1q. The crystal structure of the interaction domain of C1s has been solved and refined to 1.5 A resolution. The structure reveals a head-to-tail homodimer involving interactions between the CUB1 module of one monomer and the epidermal growth factor (EGF) module of its counterpart. A Ca2+ ion is bound to each EGF module and stabilizes both the intra- and inter-monomer interfaces. Unexpectedly, a second Ca2+ ion is bound to the distal end of each CUB1 module, through six ligands contributed by Glu45, Asp53, Asp98, and two water molecules. These acidic residues and Tyr17 are conserved in approximately two-thirds of the CUB repertoire and define a novel, Ca2+-binding CUB module subset. The C1s structure was used to build a model of the C1r-C1s CUB1-EGF heterodimer, which in C1 connects C1r to C1s and mediates interaction with C1q. A structural model of the C1q/C1r/C1s interface is proposed, where the rod-like collagen triple helix of C1q is accommodated into a groove along the transversal axis of the C1r-C1s heterodimer.

X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement.,Gregory LA, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C J Biol Chem. 2003 Aug 22;278(34):32157-64. Epub 2003 Jun 4. PMID:12788922^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gregory LA, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C. X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement. J Biol Chem. 2003 Aug 22;278(34):32157-64. Epub 2003 Jun 4. PMID:12788922 doi:http://dx.doi.org/10.1074/jbc.M305175200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nzi"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s==
 <StructureSection load='1nzi' size='340' side='right' caption='[[1nzi]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C1S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzi OCA], [http://pdbe.org/1nzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nzi RCSB], [http://www.ebi.ac.uk/pdbsum/1nzi PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzi OCA], [http://pdbe.org/1nzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nzi RCSB], [http://www.ebi.ac.uk/pdbsum/1nzi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nzi ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 16: / Line 17: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nz/1nzi_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nz/1nzi_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 42: / Line 43: @@
 [[Category: Gregory, L A]]
 [[Category: Thielens, N M]]
+[[Category: Calcium]]
 [[Category: Complement]]
 [[Category: Cub]]

1nzi

From Proteopedia

Revision as of 07:34, 7 February 2018

Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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