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2pys

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(New page: 200px<br /> <applet load="2pys" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pys, resolution 1.80&Aring;" /> '''Crystal Structure o...)
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[[Image:2pys.gif|left|200px]]<br />
 
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<applet load="2pys" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pys, resolution 1.80&Aring;" />
 
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'''Crystal Structure of a Five Site Mutated Cyanovirin-N with a Mannose Dimer Bound at 1.8 A Resolution'''<br />
 
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==Overview==
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==Crystal Structure of a Five Site Mutated Cyanovirin-N with a Mannose Dimer Bound at 1.8 A Resolution==
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Cyanovirin-N (CV-N) is a 101 amino acid cyanobacterial lectin with potent, antiviral activity against HIV, mediated by high-affinity binding to, branched N-linked oligomannosides on the viral surface envelope protein, gp120. The protein contains two carbohydrate-binding domains, A and B, each of which binds short oligomannosides independently in vitro. The, interaction to gp120 could involve either a single domain or both domains, simultaneously; it is not clear which mode would elicit the antiviral, activity. The model is complicated by the formation of a domain-swapped, dimer form, in which part of each domain is exchanged between two, monomers, which contains four functional carbohydrate-binding domains. To, clarify whether multivalent interactions with gp120 are necessary for the, antiviral activity, we engineered a novel mutant, P51G-m4-CVN, in which, the binding site on domain A has been knocked out; in addition, a [P51G], mutation prevents the formation of domain-swapped dimers under, physiological conditions. Here, we present the crystal structures at 1.8 A, of the free and of the dimannose-bound forms of P51G-m4-CVN, revealing a, monomeric structure in which only domain B is bound to dimannose., P51G-m4-CVN binds gp120 with an affinity almost 2 orders of magnitude, lower than wt CV-N and is completely inactive against HIV. The tight, binding to gp120 is recovered in the domain-swapped version of, P51G-m4-CVN, prepared under extreme conditions. Our findings show that the, presence of at least two oligomannoside-binding sites, either by the, presence of intact domains A and B or by formation of domain-swapped, dimers, is essential for activity.
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<StructureSection load='2pys' size='340' side='right'caption='[[2pys]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2pys]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PYS 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]] 1.8&#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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PRD_900111:2alpha-alpha-mannobiose'>PRD_900111</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=2pys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pys OCA], [https://pdbe.org/2pys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pys RCSB], [https://www.ebi.ac.uk/pdbsum/2pys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pys ProSAT]</span></td></tr>
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</table>
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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/py/2pys_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=2pys ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyanovirin-N (CV-N) is a 101 amino acid cyanobacterial lectin with potent antiviral activity against HIV, mediated by high-affinity binding to branched N-linked oligomannosides on the viral surface envelope protein gp120. The protein contains two carbohydrate-binding domains, A and B, each of which binds short oligomannosides independently in vitro. The interaction to gp120 could involve either a single domain or both domains simultaneously; it is not clear which mode would elicit the antiviral activity. The model is complicated by the formation of a domain-swapped dimer form, in which part of each domain is exchanged between two monomers, which contains four functional carbohydrate-binding domains. To clarify whether multivalent interactions with gp120 are necessary for the antiviral activity, we engineered a novel mutant, P51G-m4-CVN, in which the binding site on domain A has been knocked out; in addition, a [P51G] mutation prevents the formation of domain-swapped dimers under physiological conditions. Here, we present the crystal structures at 1.8 A of the free and of the dimannose-bound forms of P51G-m4-CVN, revealing a monomeric structure in which only domain B is bound to dimannose. P51G-m4-CVN binds gp120 with an affinity almost 2 orders of magnitude lower than wt CV-N and is completely inactive against HIV. The tight binding to gp120 is recovered in the domain-swapped version of P51G-m4-CVN, prepared under extreme conditions. Our findings show that the presence of at least two oligomannoside-binding sites, either by the presence of intact domains A and B or by formation of domain-swapped dimers, is essential for activity.
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==About this Structure==
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A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity.,Fromme R, Katiliene Z, Giomarelli B, Bogani F, Mc Mahon J, Mori T, Fromme P, Ghirlanda G Biochemistry. 2007 Aug 14;46(32):9199-207. Epub 2007 Jul 18. PMID:17636873<ref>PMID:17636873</ref>
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2PYS 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=2PYS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A Monovalent Mutant of Cyanovirin-N Provides Insight into the Role of Multiple Interactions with gp120 for Antiviral Activity(,)., Fromme R, Katiliene Z, Giomarelli B, Bogani F, Mahon JM, Mori T, Fromme P, Ghirlanda G, Biochemistry. 2007 Jul 18;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17636873 17636873]
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</div>
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<div class="pdbe-citations 2pys" style="background-color:#fffaf0;"></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: Fromme P]]
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[[Category: Fromme, P.]]
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[[Category: Fromme R]]
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[[Category: Fromme, R.]]
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[[Category: Ghirlanda G]]
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[[Category: Ghirlanda, G.]]
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[[Category: Katilene Z]]
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[[Category: Katilene, Z.]]
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[[Category: anti hiv]]
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[[Category: cyanovirin-n]]
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[[Category: sugar binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:56:58 2007''
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Current revision

Crystal Structure of a Five Site Mutated Cyanovirin-N with a Mannose Dimer Bound at 1.8 A Resolution

PDB ID 2pys

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