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1afk
From Proteopedia
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[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
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Revision as of 12:43, 30 October 2007
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CRYSTAL STRUCTURE OF RIBONUCLEASE A IN COMPLEX WITH 5'-DIPHOSPHOADENOSINE-3'-PHOSPHATE
Overview
High-resolution (1.7 A) crystal structures have been determined for bovine, pancreatic ribonuclease A (RNase A) complexed with 5'-diphosphoadenosine, 3'-phosphate (ppA-3'-p) and 5'-diphosphoadenosine 2'-phosphate (ppA-2'-p), as well as for a native structure refined to 2.0 A. These nucleotide, phosphates are the two most potent inhibitors of RNase A reported so far, with Ki values of 240 and 520 nM, respectively. The binding modes and, conformations of ppA-3'-p and ppA-2'-p were found to differ markedly from, those anticipated on the basis of earlier structures of RNase A complexes., The key difference is that the 5'-beta-phosphate rather than the, 5'-alpha-phosphate of each inhibitor occupies the P1 phosphate binding, site. As a consequence, the ribose moieties of the two nucleotides ... [(full description)]
About this Structure
1AFK is a [Single protein] structure of sequence from [Bos taurus] with PAP as [ligand]. Active as [Pancreatic ribonuclease], with EC number [3.1.27.5]. Structure known Active Sites: CA1 and CAT. Full crystallographic information is available from [OCA].
Reference
Crystal structures of ribonuclease A complexes with 5'-diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7 A resolution., Leonidas DD, Shapiro R, Irons LI, Russo N, Acharya KR, Biochemistry. 1997 May 6;36(18):5578-88. PMID:9154942
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