1vam

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(New page: 200px<br /><applet load="1vam" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vam, resolution 2.75&Aring;" /> '''CONCANAVALIN A COMPL...)
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[[Image:1vam.gif|left|200px]]<br /><applet load="1vam" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vam, resolution 2.75&Aring;" />
 
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'''CONCANAVALIN A COMPLEX WITH 4'-NITROPHENYL-ALPHA-D-MANNOPYRANOSIDE'''<br />
 
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==Overview==
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==CONCANAVALIN A COMPLEX WITH 4'-NITROPHENYL-ALPHA-D-MANNOPYRANOSIDE==
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Concanavalin A (Con A) is the best-known plant lectin and has important in, vitro biological activities arising from its specific saccharide-binding, ability. Its exact biological role still remains unknown. The complexes of, Con A with 4'-nitrophenyl-alpha-D-mannopyranoside (alpha-PNM) and, 4'-nitrophenyl-alpha-D-glucopyranoside (alpha-PNG) have been crystallized, in space group P2(1)2(1)2 with cell dimensions a = 135.19 A, b = 155.38 A, c = 71.25 A and a = 134.66 A, b = 155.67 A, and c = 71.42 A, respectively., X-ray diffraction intensities to 2.75 A for the alpha-PNM and to 3.0 A, resolution for the alpha-PNG complex have been collected. The structures, of the complexes were solved by molecular replacement and refined by, simulated annealing methods to crystallographic R-factor values of, 0.185/0.186 and free-R-factor values of 0.260/0.274, respectively. In both, structures, the asymmetric unit contains four molecules arranged as a, tetramer, with approximate 222 symmetry. A saccharide molecule is bound in, the sugar-binding site near the surface of each monomer. The nonsugar, (aglycon) portion of the compounds used helps to identify the exact, orientation of the saccharide in the sugar-binding pocket and is involved, in major interactions between tetramers. The hydrogen bonding network in, the region of the binding site has been analyzed, and only minor, differences with the previously reported Con, A-methyl-alpha-D-mannopyranoside complex structure have been observed., Structural differences that may contribute to the slight preference of the, lectin for mannosides over glucosides are discussed. Calculations indicate, a negative electrostatic surface potential for the saccharide binding site, of Con A, which may be important for its biological activity. It is also, shown in detail how a particular class of hydrophobic ligands interact, with one of the three so-called characteristic hydrophobic sites of the, lectins.
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<StructureSection load='1vam' size='340' side='right'caption='[[1vam]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vam]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VAM FirstGlance]. <br>
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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]] 2.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PNA:4-NITROPHENYL-ALPHA-D-MANNOPYRANOSIDE'>PNA</scene></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=1vam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vam OCA], [https://pdbe.org/1vam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vam RCSB], [https://www.ebi.ac.uk/pdbsum/1vam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vam ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
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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/va/1vam_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=1vam ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1VAM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with PNA, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VAM OCA].
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*[[Concanavalin 3D structures|Concanavalin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The crystal structure of the complexes of concanavalin A with 4'-nitrophenyl-alpha-D-mannopyranoside and 4'-nitrophenyl-alpha-D-glucopyranoside., Kanellopoulos PN, Pavlou K, Perrakis A, Agianian B, Vorgias CE, Mavrommatis C, Soufi M, Tucker PA, Hamodrakas SJ, J Struct Biol. 1996 May-Jun;116(3):345-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8812993 8812993]
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[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hamodrakas, S.J.]]
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[[Category: Hamodrakas SJ]]
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[[Category: Kanellopoulos, P.N.]]
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[[Category: Kanellopoulos PN]]
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[[Category: Tucker, P.A.]]
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[[Category: Tucker PA]]
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[[Category: CA]]
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[[Category: MN]]
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[[Category: PNA]]
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[[Category: legume lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:33:20 2007''
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Current revision

CONCANAVALIN A COMPLEX WITH 4'-NITROPHENYL-ALPHA-D-MANNOPYRANOSIDE

PDB ID 1vam

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