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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 29, Number 11
BKCSDE 29(11)
November 20, 2008 

NMR Assignment of des [40-93] Mutant of Bovine Angiogenin
Woonghee Kim, Sun Hee Back, Dong Il Kang, Hang Cheol Shin, Yangmee Kim*,
Angiogenin, des [40-93], NMR, Assignment, Angiogenesis
Angiogenin is a potent inducer of blood vessel formation and is overexpressed in many cancers. It is a member of the pancreatic RNase superfamily. Angiogenin has 33% sequence identity with RNase A. All RNases family proteins except angiogenin and turtle RNase have four disulfide bonds. Angiogenin has three disulfide bonds, [C27-C82], [C40-C93] and [C58-C108], respectively. To examine the role of disulfide bond [C40-C93] near the nuclear localization site, recombinant des [40-93] mutant by replacement of cysteines at positions 40 and 93 with serines was cloned, expressed, and purified. CD spectrum of des [40-93] was similar to that of wild type and implies that the overall folding of two forms is similar. 2D and 3D NMR experiments for 15N and/or 13C-isotope labeled des [40-93] were performed and the backbone resonance assignment was done. Based on the result of backbone assignment and chemical shift index (CSI), we confirmed that deletion of [C40-C93] disulfide bond affected the local structural stability of bovine angiogenin near the nuclear localization site and ribonucleolytic active site. Based on this assignment, studies on structure and dynamics of des [40-93] mutant will be performed.
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