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Crystal structure of the dimeric unswapped form of bovine seminal ribonuclease

✍ Scribed by R Berisio; F Sica; C De Lorenzo; A Di Fiore; R Piccoli; A Zagari; L Mazzarella


Book ID
117105902
Publisher
Elsevier Science
Year
2003
Tongue
English
Weight
301 KB
Volume
554
Category
Article
ISSN
0014-5793

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We report here the refinement at 2.5-A resolution of the x-ray crystal structure of bovine seminal rihonuclease, a dimeric covalent enzyme. The protein, which crystallizes with one molecule in the asymmetric unit, consists of two subunits of identical chemical sequences, related by an almost exact b

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## Abstract Bovine seminal ribonuclease (BS‐RNase) is a unique member of the pancreatic‐like ribonuclease superfamily. This enzyme exists as two conformational isomers with distinctive biological properties. The structure of the major isomer is characterized by the swapping of the N‐terminal segmen