| Structural highlights
1w4p is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Related: | 1a2w, 1a5p, 1a5q, 1afk, 1afl, 1afu, 1aqp, 1b6v, 1bel, 1bzq, 1c0b, 1c0c, 1c8w, 1c9v, 1c9x, 1cjq, 1cjr, 1d5d, 1d5e, 1d5h, 1dfj, 1dy5, 1eic, 1eid, 1eie, 1eos, 1eow, 1f0v, 1fev, 1fs3, 1gv7, 1izp, 1izq, 1izr, 1j7z, 1j80, 1j81, 1j82, 1jn4, 1js0, 1jvt, 1jvu, 1jvv, 1kf2, 1kf3, 1kf4, 1kf5, 1kf7, 1kf8, 1kh8, 1lsq, 1o0f, 1o0h, 1o0m, 1o0n, 1o0o, 1qhc, 1rar, 1ras, 1rat, 1rbb, 1rbc, 1rbd, 1rbe, 1rbf, 1rbg, 1rbh, 1rbi, 1rbj, 1rbn, 1rbw, 1rbx, 1rca, 1rcn, 1rha, 1rhb, 1rnc, 1rnd, 1rnm, 1rnn, 1rno, 1rnq, 1rnu, 1rnv, 1rnw, 1rnx, 1rny, 1rnz, 1rob, 1rpf, 1rpg, 1rph, 1rsm, 1rta, 1rtb, 1ruv, 1srn, 1ssa, 1ssb, 1ssc, 1un5, 1w4o, 1w4q, 1xps, 1xpt, 2aas, 2rat, 2rln, 2rns, 3rat, 3rn3, 3rsd, 3rsk, 3rsp, 3srn, 4rat, 4rsd, 4rsk, 4srn, 5rat, 5rsa, 6rat, 6rsa, 7rat, 7rsa, 8rat, 8rsa, 9rat, 9rsa |
| Activity: | Pancreatic ribonuclease, with EC number 3.1.27.5 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
2'-Fluoro-2'-deoxyuridine 3'-phosphate (dU(F)MP) and arabinouridine 3'-phosphate (araUMP) have non-natural furanose rings. dU(F)MP and araUMP were prepared by chemical synthesis and found to have three- to sevenfold higher affinity than uridine 3'-phosphate (3'-UMP) or 2'-deoxyuridine 3'-phosphate (dUMP) for ribonuclease A (RNase A). These differences probably arise (in part) from the phosphoryl groups of 3'-UMP, dU(F)MP, and araUMP (pK(a) = 5.9) being more anionic than that of dUMP (pK(a) = 6.3). The three-dimensional structures of the crystalline complexes of RNase A with dUMP, dU(F)MP and araUMP were determined at < 1.7 A resolution by X-ray diffraction analysis. In these three structures, the uracil nucleobases and phosphoryl groups bind to the enzyme in a nearly identical position. Unlike 3'-UMP and dU(F)MP, dUMP and araUMP bind with their furanose rings in the preferred pucker. In the RNase A.araUMP complex, the 2'-hydroxyl group is exposed to the solvent. All four 3'-nucleotides bind more tightly to wild-type RNase A than to its T45G variant, which lacks the residue that interacts most closely with the uracil nucleobase. These findings illuminate in atomic detail the interaction of RNase A and 3'-nucleotides, and indicate that non-natural furanose rings can serve as the basis for more potent inhibitors of catalysis by RNase A.
Binding of non-natural 3'-nucleotides to ribonuclease A.,Jenkins CL, Thiyagarajan N, Sweeney RY, Guy MP, Kelemen BR, Acharya KR, Raines RT FEBS J. 2005 Feb;272(3):744-55. PMID:15670155[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
- ↑ Jenkins CL, Thiyagarajan N, Sweeney RY, Guy MP, Kelemen BR, Acharya KR, Raines RT. Binding of non-natural 3'-nucleotides to ribonuclease A. FEBS J. 2005 Feb;272(3):744-55. PMID:15670155 doi:http://dx.doi.org/10.1111/j.1742-4658.2004.04511.x
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