2kjl: Difference between revisions
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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]], [[NMR_Ensembles_of_Models | 30 NMR models]]' 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 [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> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Tubbo]] | [[Category: Tubbo]] | ||
[[Category: Gronenborn, A M]] | [[Category: Gronenborn, A M]] | ||
Revision as of 12:37, 26 February 2020
NMR structures of a designed Cyanovirin-N homolog lectin; LKAMGNMR structures of a designed Cyanovirin-N homolog lectin; LKAMG
Structural highlights
Function[CVNH_TUBBO] 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 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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