2qy0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:42, 30 August 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2qy0.png|left|200px]]
 
-
<!--
+
==Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts==
-
The line below this paragraph, containing "STRUCTURE_2qy0", creates the "Structure Box" on the page.
+
<StructureSection load='2qy0' size='340' side='right'caption='[[2qy0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2qy0]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QY0 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-
{{STRUCTURE_2qy0| PDB=2qy0 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qy0 OCA], [https://pdbe.org/2qy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qy0 RCSB], [https://www.ebi.ac.uk/pdbsum/2qy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qy0 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/C1R_HUMAN C1R_HUMAN] C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/2qy0_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qy0 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts===
+
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<ref>PMID:17996945</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_17996945}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2qy0" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 17996945 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_17996945}}
+
__TOC__
-
 
+
</StructureSection>
-
==Disease==
+
-
Known disease associated with this structure: C1r/C1s deficiency, combined OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=216950 216950]]
+
-
 
+
-
==About this Structure==
+
-
2QY0 is a 4 chains 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==
+
-
<ref group="xtra">PMID:17996945</ref><references group="xtra"/>
+
-
[[Category: Complement subcomponent C1r]]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Barabas, O.]]
+
[[Category: Large Structures]]
-
[[Category: Gal, P.]]
+
[[Category: Barabas O]]
-
[[Category: Goto, Y.]]
+
[[Category: Gal P]]
-
[[Category: Graf, L.]]
+
[[Category: Goto Y]]
-
[[Category: Harmat, V.]]
+
[[Category: Graf L]]
-
[[Category: Kardos, J.]]
+
[[Category: Harmat V]]
-
[[Category: Naray-Szabo, G.]]
+
[[Category: Kardos J]]
-
[[Category: Pallo, A.]]
+
[[Category: Naray-Szabo G]]
-
[[Category: Szilagyi, K.]]
+
[[Category: Pallo A]]
-
[[Category: Zavodszky, P.]]
+
[[Category: Szilagyi K]]
-
[[Category: Beta barrel]]
+
[[Category: Zavodszky P]]
-
[[Category: Complement]]
+
-
[[Category: Complement pathway]]
+
-
[[Category: Egf-like domain]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Hydroxylation]]
+
-
[[Category: Immune response]]
+
-
[[Category: Innate immunity]]
+
-
[[Category: Phosphorylation]]
+
-
[[Category: Polymorphism]]
+
-
[[Category: Serine protease]]
+
-
[[Category: Sushi]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:34:44 2009''
+

Current revision

Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts

PDB ID 2qy0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qy0"
Personal tools