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1oqs

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[[Image:1oqs.gif|left|200px]]
 
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==Crystal Structure of RV4/RV7 Complex==
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The line below this paragraph, containing "STRUCTURE_1oqs", creates the "Structure Box" on the page.
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<StructureSection load='1oqs' size='340' side='right'caption='[[1oqs]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1oqs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_siamensis Daboia siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OQS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqs OCA], [https://pdbe.org/1oqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oqs RCSB], [https://www.ebi.ac.uk/pdbsum/1oqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqs ProSAT]</span></td></tr>
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{{STRUCTURE_1oqs| PDB=1oqs | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA2A7_DABSI PA2A7_DABSI] Heterodimer: RV-4/RV-7 targets the presynaptic sites of the neuromuscular junction.<ref>PMID:8835338</ref> Monomer: snake venom phospholipase A2 (PLA2) RV-7 that has low enzymatic activity and is not toxic. It inhibits the enzymatic activity of RV-4 in vitro but potentiates its lethal potency and neurotoxicity. It may facilitate the specific binding of RV-4 to its presynaptic binding sites, probably by acting as a chaperon, minimizing distraction and destruction of RV-4 en route to the site of action by reducing non-specific binding to muscle and other organs. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:8835338</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/1oqs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1oqs ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of RV4/RV7 Complex'''
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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==Overview==
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<references/>
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The presynaptic viperotoxin F is the major lethal component of the venom of Vipera russelli formosensis (Taiwan viper). It is a heterodimer of two highly homologous (65% identity) but oppositely charged subunits: a basic and neurotoxic PLA(2) (RV-4) and an acidic non-toxic component with a very low enzymatic activity (RV-7). The crystal structure of the complex has been determined by molecular replacement and refined to 1.9 A resolution and an R factor of 22.3% with four RV-4/RV-7 complexes in the asymmetric unit, which do not exhibit any local point-group symmetry. The complex formation decreases the accessible surface area of the two subunits by approximately 1425 A(2). Both PLA(2)s are predicted to have very low, if any, anticoagulant activity. The structure of viperotoxin F is compared with that of the heterodimeric neurotoxin vipoxin from the venom of another viper, V. ammodytes meridionalis. The structural basis for the differences between the pharmacological activities of the two toxins is discussed. The neutralization of the negative charge of the major ligand for Ca(2+), Asp49, by intersubunit salt bridges is probably a common mechanism of self-stabilization of heterodimeric Viperinae snake-venom neurotoxins in the absence of bound calcium.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Daboia siamensis]]
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1OQS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Daboia_russellii_siamensis Daboia russellii siamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQS OCA].
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[[Category: Large Structures]]
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[[Category: Betzel C]]
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==Reference==
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[[Category: Perbandt M]]
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Structure of the heterodimeric neurotoxic complex viperotoxin F (RV-4/RV-7) from the venom of Vipera russelli formosensis at 1.9 A resolution., Perbandt M, Tsai IH, Fuchs A, Banumathi S, Rajashankar KR, Georgieva D, Kalkura N, Singh TP, Genov N, Betzel C, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1679-87. Epub 2003, Sep 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14501106 14501106]
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[[Category: Daboia russellii siamensis]]
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[[Category: Protein complex]]
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[[Category: Betzel, C.]]
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[[Category: Perbandt, M.]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:10:19 2008''
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Current revision

Crystal Structure of RV4/RV7 Complex

PDB ID 1oqs

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