NDLI: Sequence-specific backbone $^{1}$H, $^{13}$C, and $^{15}$N resonance assignments of human ribonuclease 4

Content Provider	Springer Nature Link
Author	Gagné, Donald Doucet, Nicolas
Copyright Year	2014
Abstract	Human ribonuclease 4 (RNase 4) is the most evolutionarily conserved member of the 8 canonical human pancreatic-like RNases, showing more than 90 % identity with bovine and porcine homologues. The enzyme displays ribonucleolytic activity with a strong preference for uracil-containing RNA substrates, a feature only shared with human eosinophil derived-neurotoxin (EDN, or RNase 2) and eosinophil cationic protein (ECP, or RNase 3). It is also the shortest member of the human family, with a significantly truncated C-terminal tail. Its unique active-site pocket and high degree of conservation among vertebrates suggest that the enzyme plays a crucial biological function. Here, we report on the $^{1}$H, $^{13}$C and $^{15}$N backbone resonance assignments of RNase 4, providing means to characterize its molecular function at the atomic level by NMR.
Starting Page	181
Ending Page	185
Page Count	5
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	9
Issue Number	1
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2014-07-17
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Orthologues Ribonucleases RNase A Evolutionary conservation RNA Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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Sequence-specific backbone $^{1}$H, $^{13}$C, and $^{15}$N resonance assignments of human ribonuclease 4