1uos

From Proteopedia

(Difference between revisions)

Current revision

The Crystal Structure of the Snake Venom Toxin Convulxin

Structural highlights

1uos is a 4 chain structure with sequence from Crotalus durissus terrificus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SLA_CRODU Snake venom lectin that activates platelets by binding to the platelet collagen receptor glycoprotein VI (GP6) (PubMed:9153205). The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also induced by the toxin is upstream the cytoskeletal translocation of GPIb, FcRgamma (FCER1G) and 14-3-3zeta (YWHAZ)(PubMed:16102113).^[1] ^[2]

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

Snake venoms contain a number of proteins that interact with components of the haemostatic system that promote or inhibit events leading to blood-clot formation. The snake-venom protein convulxin (Cvx) binds glycoprotein (GP) VI, the platelet receptor for collagen, and triggers signal transduction. Here, the 2.7 A resolution crystal structure of Cvx is presented. In common with other members of this snake-venom protein family, Cvx is an alphabeta-heterodimer and conforms to the C-type lectin-fold topology. Comparison with other family members allows a set of Cvx residues that form a concave surface to be putatively implicated in GPVI binding. Unlike other family members, with the exception of flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric structure is consistent with Cvx clustering GPVI molecules on the surface of platelets and as a result promoting signal transduction activity. The Cvx structure and the location of the putative binding sites suggest a model for this multimeric signalling assembly.

Structure of the snake-venom toxin convulxin.,Batuwangala T, Leduc M, Gibbins JM, Bon C, Jones EY Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):46-53. Epub 2003, Dec 18. PMID:14684891^[3]

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

References

↑ Polgar J, Clemetson JM, Kehrel BE, Wiedemann M, Magnenat EM, Wells TN, Clemetson KJ. Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. J Biol Chem. 1997 May 23;272(21):13576-83. PMID:9153205
↑ Lu Q, Clemetson JM, Clemetson KJ. Translocation of GPIb and Fc receptor gamma-chain to cytoskeleton in mucetin-activated platelets. J Thromb Haemost. 2005 Sep;3(9):2065-76. PMID:16102113 doi:http://dx.doi.org/10.1111/j.1538-7836.2005.01481.x
↑ Batuwangala T, Leduc M, Gibbins JM, Bon C, Jones EY. Structure of the snake-venom toxin convulxin. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):46-53. Epub 2003, Dec 18. PMID:14684891

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1uos.png|left|200px]]
-<!--
+==The Crystal Structure of the Snake Venom Toxin Convulxin==
-The line below this paragraph, containing "STRUCTURE_1uos", creates the "Structure Box" on the page.
+<StructureSection load='1uos' size='340' side='right'caption='[[1uos]], [[Resolution|resolution]] 2.70&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'>[[1uos]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UOS 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]] 2.7&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uos OCA], [https://pdbe.org/1uos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uos RCSB], [https://www.ebi.ac.uk/pdbsum/1uos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uos ProSAT]</span></td></tr>
-{{STRUCTURE_1uos|  PDB=1uos  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SLA_CRODU SLA_CRODU] Snake venom lectin that activates platelets by binding to the platelet collagen receptor glycoprotein VI (GP6) (PubMed:9153205). The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also induced by the toxin is upstream the cytoskeletal translocation of GPIb, FcRgamma (FCER1G) and 14-3-3zeta (YWHAZ)(PubMed:16102113).<ref>PMID:9153205</ref> <ref>PMID:16102113</ref>
+== 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/uo/1uos_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1uos ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Snake venoms contain a number of proteins that interact with components of the haemostatic system that promote or inhibit events leading to blood-clot formation. The snake-venom protein convulxin (Cvx) binds glycoprotein (GP) VI, the platelet receptor for collagen, and triggers signal transduction. Here, the 2.7 A resolution crystal structure of Cvx is presented. In common with other members of this snake-venom protein family, Cvx is an alphabeta-heterodimer and conforms to the C-type lectin-fold topology. Comparison with other family members allows a set of Cvx residues that form a concave surface to be putatively implicated in GPVI binding. Unlike other family members, with the exception of flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric structure is consistent with Cvx clustering GPVI molecules on the surface of platelets and as a result promoting signal transduction activity. The Cvx structure and the location of the putative binding sites suggest a model for this multimeric signalling assembly.
-===THE CRYSTAL STRUCTURE OF THE SNAKE VENOM TOXIN CONVULXIN===
+Structure of the snake-venom toxin convulxin.,Batuwangala T, Leduc M, Gibbins JM, Bon C, Jones EY Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):46-53. Epub 2003, Dec 18. PMID:14684891<ref>PMID:14684891</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_14684891}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1uos" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 14684891 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14684891}}
+__TOC__
+</StructureSection>
-==About this Structure==
-UOS is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UOS OCA].
-==Reference==
-<ref group="xtra">PMID:14684891</ref><references group="xtra"/>
 [[Category: Crotalus durissus terrificus]]
-[[Category: Batuwangala, T.]]
+[[Category: Large Structures]]
-[[Category: Bon, C.]]
+[[Category: Batuwangala T]]
-[[Category: Gibbins, J M.]]
+[[Category: Bon C]]
-[[Category: Jones, E Y.]]
+[[Category: Gibbins JM]]
-[[Category: Leduc, M.]]
+[[Category: Jones EY]]
-[[Category: C-type lectin]]
+[[Category: Leduc M]]
-[[Category: Convulxin]]
-[[Category: Gpvi]]
-[[Category: Lectin]]
-[[Category: Snake toxin]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]
-[[Category: Sugar-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 17 08:56:25 2009''

1uos

From Proteopedia

Current revision

The Crystal Structure of the Snake Venom Toxin Convulxin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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