2jzk: Difference between revisions
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[[Image: | ==Structure of TbCVNH (T. BORCHII CVNH) (CASP TARGET)== | ||
<StructureSection load='2jzk' size='340' side='right' caption='[[2jzk]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jzk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tuber_borchii Tuber borchii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JZK FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jzj|2jzj]], [[2jzl|2jzl]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jzk RCSB], [http://www.ebi.ac.uk/pdbsum/2jzk PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jzk_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Tuber borchii]] | [[Category: Tuber borchii]] | ||
[[Category: Gronenborn, A M.]] | [[Category: Gronenborn, A M.]] | ||
Revision as of 13:56, 30 September 2014
Structure of TbCVNH (T. BORCHII CVNH) (CASP TARGET)Structure of TbCVNH (T. BORCHII CVNH) (CASP TARGET)
Structural highlights
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 PubMedSolution 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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