View source for 2pjf


==Solution structure of rhodostomin==
<StructureSection load='2pjf' size='340' side='right'caption='[[2pjf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pjf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agkistrodon_rhodostoma Agkistrodon rhodostoma]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jyp 1jyp]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PJF FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RHOD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8717 Agkistrodon rhodostoma])</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=2pjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pjf OCA], [https://pdbe.org/2pjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pjf RCSB], [https://www.ebi.ac.uk/pdbsum/2pjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pjf ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/VM2RH_CALRH VM2RH_CALRH]] Metalloproteinase rhodostoxin: snake venom metalloproteinase that impairs hemostasis in the envenomed animal (By similarity).  Disintegrin rhodostomin: inhibit platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). 
== 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/pj/2pjf_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=2pjf ConSurf].
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== Publication Abstract from PubMed ==
Rhodostomin (Rho) is a snake venom protein containing an RGD motif that specifically inhibits the integrin-binding function. Rho produced in Pichia pastoris inhibits platelet aggregation with a K(I) of 78 nM as potent as native Rho. In contrast, its D51E mutant inhibits platelet aggregation with a K(I) of 49 muM. Structural analysis of Rho and its D51E mutant showed that they have the same tertiary fold with three two-stranded antiparallel beta-sheets. There are no structural backbone differences between the RG[D/E] loop which extends outward from the protein core and the RG[D/E] sequence at its apex in a four-residue RG[D/E]M type I turn. Two minor differences between Rho and its D51E mutant were only found from their backbone dynamics and 3D structures. The R(2) value of E51 is 13% higher than that of the D51 residue. A difference in the charge separation of 1.76 A was found between the sidechains of positive (R49) and negative residues (D51 or E51).The docking of Rho into integrin alphavbeta3 showed that the backbone amide and carbonyl groups of the D51 residue of Rho were formed hydrogen bonds with the integrin residues R216 and R214, respectively. In contrast, these hydrogen bonds were absent in the D51E mutant-integrin complex. Our findings suggest that the interactions between both the sidechain and backbone of the D residue of RGD-containing ligands and integrin are important for their binding. Proteins 2009. (c) 2009 Wiley-Liss, Inc.

Effect of D to E mutation of the RGD motif in rhodostomin on its activity, structure, and dynamics: Importance of the interactions between the D residue and integrin.,Chen CY, Shiu JH, Hsieh YH, Liu YC, Chen YC, Chen YC, Jeng WY, Tang MJ, Lo SJ, Chuang WJ Proteins. 2009 Feb 2. PMID:19280603<ref>PMID:19280603</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2pjf" style="background-color:#fffaf0;"></div>

==See Also==
*[[Disintegrin|Disintegrin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Agkistrodon rhodostoma]]
[[Category: Large Structures]]
[[Category: Chang, Y T]]
[[Category: Chen, C Y]]
[[Category: Chen, Y C]]
[[Category: Chuang, W J]]
[[Category: Disintegrin]]
[[Category: Hydrolase]]
[[Category: Rhodostomin]]