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==NMR structures of a designed Cyanovirin-N homolog lectin; LKAMG==
==NMR structures of a designed Cyanovirin-N homolog lectin; LKAMG==
<StructureSection load='2kjl' size='340' side='right'caption='[[2kjl]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
<StructureSection load='2kjl' size='340' side='right'caption='[[2kjl]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kjl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tubbo Tubbo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KJL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KJL FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kjl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] and [https://en.wikipedia.org/wiki/Tuber_borchii Tuber borchii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KJL FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kjl OCA], [http://pdbe.org/2kjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kjl RCSB], [http://www.ebi.ac.uk/pdbsum/2kjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kjl ProSAT]</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kjl OCA], [https://pdbe.org/2kjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kjl RCSB], [https://www.ebi.ac.uk/pdbsum/2kjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kjl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CVNH_TUBBO CVNH_TUBBO]] Mannose-binding lectin.<ref>PMID:18400178</ref>
[https://www.uniprot.org/uniprot/CVNH_NEUCR CVNH_NEUCR] Mannose-binding lectin.<ref>PMID:18400178</ref> [https://www.uniprot.org/uniprot/CVNH_TUBBO CVNH_TUBBO] Mannose-binding lectin.<ref>PMID:18400178</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2kjl 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=2kjl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Solution structures for three members of the recently discovered cyanovirin-N (CV-N) homolog family of lectins have been determined. Cyanovirin-N homologs (CVNHs) from Tuber borchii, Ceratopteris richardii, and Neurospora crassa, representing each of the three phylogenetic groups, were selected. All proteins exhibit the same fold, and the overall structures resemble that of the founding member of the family, CV-N, albeit with noteworthy differences in loop conformation and detailed local structure. Since no data are available regarding the proteins' function or their natural ligands, extensive carbohydrate-binding studies were conducted. We delineated ligand-binding sites on all three proteins by nuclear magnetic resonance and identified which sugars interact by array screening. The number and location of binding sites vary for the three proteins, and different ligand specificities exist. Potential physiological roles for two family members, TbCVNH and NcCVNH, were probed in nutrition deprivation experiments that suggest a possible involvement of these proteins in lifestyle-related responses.
The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity.,Koharudin LM, Viscomi AR, Jee JG, Ottonello S, Gronenborn AM Structure. 2008 Apr;16(4):570-84. PMID:18400178<ref>PMID:18400178</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kjl" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Tubbo]]
[[Category: Neurospora crassa]]
[[Category: Gronenborn, A M]]
[[Category: Tuber borchii]]
[[Category: Koharudin, L M.I]]
[[Category: Gronenborn AM]]
[[Category: Cvnh]]
[[Category: Koharudin LMI]]
[[Category: Cyanovirin-n]]
[[Category: Lectin]]
[[Category: Sugar binding protein]]

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