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- | ==Structure of NcCVNH (N. CRASSA CVNH) (CASP TARGET)== | + | ==Structure of NcCVNH (N. CRASSA CVNH)== |
- | <StructureSection load='2jzl' size='340' side='right'caption='[[2jzl]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='2jzl' size='340' side='right'caption='[[2jzl]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2jzl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JZL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JZL FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jzj|2jzj]], [[2jzk|2jzk]]</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'>[http://proteopedia.org/fgij/fg.htm?mol=2jzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzl OCA], [http://pdbe.org/2jzl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jzl RCSB], [http://www.ebi.ac.uk/pdbsum/2jzl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzl ProSAT]</span></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=2jzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzl OCA], [https://pdbe.org/2jzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jzl RCSB], [https://www.ebi.ac.uk/pdbsum/2jzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzl ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/CVNH_NEUCR CVNH_NEUCR]] Mannose-binding lectin.<ref>PMID:18400178</ref> | + | [https://www.uniprot.org/uniprot/CVNH_NEUCR CVNH_NEUCR] 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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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Chrysonilia crassa]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Gronenborn, A M]] | + | [[Category: Neurospora crassa]] |
- | [[Category: Jee, J]] | + | [[Category: Gronenborn AM]] |
- | [[Category: Koharudin, L M.I]] | + | [[Category: Jee J]] |
- | [[Category: Ottonello, S]] | + | [[Category: Koharudin LMI]] |
- | [[Category: Viscomi, A R]] | + | [[Category: Ottonello S]] |
- | [[Category: Antiviral protein]]
| + | [[Category: Viscomi AR]] |
- | [[Category: Carbohydrate binding protein]]
| + | |
- | [[Category: Cvnh]]
| + | |
| Structural highlights
Function
CVNH_NEUCR Mannose-binding lectin.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Koharudin LM, Viscomi AR, Jee JG, Ottonello S, Gronenborn AM. The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity. Structure. 2008 Apr;16(4):570-84. PMID:18400178 doi:10.1016/j.str.2008.01.015
- ↑ Koharudin LM, Viscomi AR, Jee JG, Ottonello S, Gronenborn AM. The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity. Structure. 2008 Apr;16(4):570-84. PMID:18400178 doi:10.1016/j.str.2008.01.015
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