Specific protein-nucleic acid recognition in ribonuclease T1–2′-guanylic acid complex: an X-ray study View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-09

AUTHORS

Udo Heinemann, Wolfram Saenger

ABSTRACT

RNase T1 is folded into an alpha-helix of 4.5 turns, covered by a four-strand antiparallel beta-sheet. Specific recognition of 2'-guanylic acid arises from hydrogen bonding between main chain peptide groups and the O-6 and N-1-H of guanine, as well as from stacking of Tyr 45 on guanine. At the active site, Glu 58, His 92 and Arg 77 are involved in phosphodiester hydrolysis. More... »

PAGES

27-31

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/299027a0

DOI

http://dx.doi.org/10.1038/299027a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1039891089

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6287278


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