1mr6: Difference between revisions

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 ==Solution Structure of gamma-Bungarotoxin:Implication for the role of the Residues Adjacent to RGD in Integrin Binding==
-<StructureSection load='1mr6' size='340' side='right' caption='[[1mr6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1mr6' size='340' side='right'caption='[[1mr6]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mr6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MR6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mr6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MR6 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mr6 RCSB], [http://www.ebi.ac.uk/pdbsum/1mr6 PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr6 OCA], [https://pdbe.org/1mr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1mr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/3NO5I_BUNMU 3NO5I_BUNMU] Exhibits M2 muscarinic acetylcholine receptor (CHRM2)-blocking activity, but has a weak binding activity toward nicotinic AChR. Moreover, it inhibits collagen-induced platelet aggregation.<ref>PMID:12168693</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/mr/1mr6_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mr6_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1mr6 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Gamma-bungarotoxin, a snake venom protein isolated from Bungarus multicinctus, contains 68 amino acids, including 10 cysteine residues and a TAVRGDGP sequence at positions 30-37. The solution structure of gamma-bungarotoxin has been determined by nuclear magnetic resonance (NMR) spectroscopy. The structure is similar to that of the short-chain neurotoxins that contain three loops extending from a disulfide-bridged core. The tripeptide Arg-Gly-Asp (RGD) sequence is located at the apex of the flexible loop and is similar to that of other RGD-containing proteins. However, gamma-bungarotoxin only inhibits platelet aggregations with an IC50 of 34 microM. To understand its weak activity in inhibiting platelet aggregation, we mutated the RGD loop sequences of rhodostomin, a potent platelet aggregation inhibitor, from RIPRGDMP to TAVRGDGP, resulting in a 196-fold decrease in activity. In addition, the average Calpha-to-Calpha distance between R33 and G36 of gamma-bungarotoxin is 6.02 A, i.e., shorter than that of other RGD-containing proteins that range from 6.55 to 7.46 A. These results suggested that the amino acid residues flanking the RGD motif might control the width of the RGD loop. This structural difference may be responsible for its decrease in platelet aggregation inhibition compared with other RGD-containing proteins.
-Solution structure of gamma-bungarotoxin: the functional significance of amino acid residues flanking the RGD motif in integrin binding.,Shiu JH, Chen CY, Chang LS, Chen YC, Chen YC, Lo YH, Liu YC, Chuang WJ Proteins. 2004 Dec 1;57(4):839-49. PMID:15390258<ref>PMID:15390258</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Bungarotoxin|Bungarotoxin]]
+*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
 == References ==
 <references/>
@@ Line 31: / Line 27: @@
 </StructureSection>
 [[Category: Bungarus multicinctus]]
-[[Category: Chang, L S.]]
+[[Category: Large Structures]]
-[[Category: Chen, C Y.]]
+[[Category: Chang L-S]]
-[[Category: Chen, Y C.]]
+[[Category: Chen C-Y]]
-[[Category: Chuang, W J.]]
+[[Category: Chen Y-C]]
-[[Category: Shiu, J H.]]
+[[Category: Chuang W-J]]
-[[Category: Neurotoxin]]
+[[Category: Shiu J-H]]
-[[Category: Toxin]]
-[[Category: Venom]]