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1n02

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(New page: 200px<br /> <applet load="1n02" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n02" /> '''Solution Structure of a Circular-Permuted V...)
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[[Image:1n02.gif|left|200px]]<br />
 
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<applet load="1n02" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n02" />
 
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'''Solution Structure of a Circular-Permuted Variant of the Potent HIV-inactivating Protein Cyanovirin-N'''<br />
 
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==Overview==
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==Solution Structure of a Circular-Permuted Variant of the Potent HIV-inactivating Protein Cyanovirin-N==
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The high-resolution solution structure of a monomeric circular permuted, (cp) variant of the potent HIV-inactivating protein cyanovirin-N (CV-N), was determined by NMR. Comparison with the wild-type (wt) structure, revealed that the observed loss in stability of cpCV-N compared to the wt, protein is due to less favorable packing of several residues at the pseudo, twofold axis that are responsible for holding the two halves of the, molecule together. In particular, the N and C-terminal amino acid residues, exhibit conformational flexibility, resulting in fewer and less favorable, contacts between them. The important hydrophobic and hydrogen-bonding, network between residues W49, D89, H90, Y100 and E101 that was observed in, wt CV-N is no longer present. For instance, Y100 and E101 are flexible and, the tryptophan side-chain is in a different conformation compared to the, wt protein. The stability loss amounts to approximately 2kcal/mol and the, mobility of the protein is evident by fast amide proton exchange, throughout the chain. Mutation of the single proline residue to glycine, (P52G) did not substantially affect the stability of the protein, in, contrast to the finding for wtCV-N. The binding of high-mannose type, oligosaccharides to cpCV-N was also investigated. Similar to wtCV-N, two, carbohydrate-binding sites were identified on the protein and the Man, alpha1--&gt;2Man linked moieties on the sugar were delineated as binding, epitopes. Unlike in wtCV-N, the binding sites on cpCV-N are structurally, similar and exhibit comparable binding affinities for the respective, sugars. On the basis of the studies presented here and previous results on, high-mannose binding to wtCV-N, we discuss a model for the interaction, between gp120 and CV-N.
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<StructureSection load='1n02' size='340' side='right'caption='[[1n02]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1n02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N02 FirstGlance]. <br>
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1N02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N02 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1n02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n02 OCA], [https://pdbe.org/1n02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n02 RCSB], [https://www.ebi.ac.uk/pdbsum/1n02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n02 ProSAT]</span></td></tr>
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==Reference==
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</table>
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Solution structure of a circular-permuted variant of the potent HIV-inactivating protein cyanovirin-N: structural basis for protein stability and oligosaccharide interaction., Barrientos LG, Louis JM, Ratner DM, Seeberger PH, Gronenborn AM, J Mol Biol. 2003 Jan 3;325(1):211-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12473463 12473463]
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== Function ==
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[https://www.uniprot.org/uniprot/CVN_NOSEL CVN_NOSEL] Mannose-binding lectin.<ref>PMID:9210678</ref> <ref>PMID:12678493</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/n0/1n02_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=1n02 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Nostoc ellipsosporum]]
[[Category: Nostoc ellipsosporum]]
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[[Category: Single protein]]
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[[Category: Barrientos LG]]
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[[Category: Barrientos, L.G.]]
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[[Category: Gronenborn AM]]
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[[Category: Gronenborn, A.M.]]
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[[Category: virus/viral protein inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:20:57 2007''
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Current revision

Solution Structure of a Circular-Permuted Variant of the Potent HIV-inactivating Protein Cyanovirin-N

PDB ID 1n02

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