| Structural highlights
2xog 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: | 1ssb, 1afu, 1w4q, 1c0b, 6rat, 1ymr, 1o0o, 8rsa, 5rsa, 2w5l, 1rno, 7rat, 1izq, 1eid, 1cjq, 1eos, 1rnn, 1j82, 1qhc, 1ymw, 1o0h, 1afk, 1f0v, 1dy5, 1rnq, 1jn4, 1rnm, 1rbf, 1z3m, 1rnx, 1rob, 1rbn, 1rbx, 1eow, 1rbi, 7rsa, 1rbj, 1dfj, 1rsm, 1kf5, 1xps, 1rat, 1fev, 2aas, 1rhb, 1j80, 3srn, 1b6v, 1fs3, 1rpg, 1z6s, 1kf8, 1rtb, 4rsk, 1bzq, 9rsa, 1bel, 1kf4, 1kf7, 1rbw, 9rat, 1eie, 1rpf, 1o0m, 1c8w, 1rnc, 1rca, 1c0c, 1jvt, 3rsd, 1xpt, 1rbb, 2blz, 3rsp, 1ssc, 8rat, 2apq, 1j7z, 1w4o, 1rbd, 1rnz, 1jvv, 1rar, 1kf3, 1z3l, 1aqp, 1rbh, 2w5m, 1rbg, 1o0n, 1js0, 3rsk, 1ssa, 1cjr, 1eic, 1d5d, 1ymn, 1j81, 1rnw, 2w5k, 1rph, 2rns, 1rta, 1rnu, 1rny, 1z3p, 1gv7, 1rcn, 1rnv, 4rat, 1w4p, 4rsd, 1a5p, 1wbu, 1rha, 1ras, 2blp, 1rnd, 1kf2, 1d5h, 1srn, 1d5e, 2rat, 1izp, 2w5g, 1o0f, 1izr, 1c9x, 2rln, 4srn, 1c9v, 1u1b, 5rat, 1ruv, 1rbc, 2w5i, 1afl, 1z6d, 1rbe, 1a5q, 1kh8, 1lsq, 1jvu, 1a2w, 3rn3, 3rat |
| Activity: | Pancreatic ribonuclease, with EC number 3.1.27.5 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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]
Publication Abstract from PubMed
Molecular probes are useful for both studying and controlling the functions of enzymes and other proteins. The most useful probes have high affinity for their target, along with small size and resistance to degradation. Here, we report on new surrogates for nucleic acids that fulfill these criteria. Isosteres in which phosphoryl [R-O-P(O(2) (-) )-O-R'] groups are replaced with N-acylsulfonamidyl [R-C(O)-N(-) -S(O(2) )-R'] or sulfonimidyl [R-S(O(2) )-N(-) -S(O(2) )-R'] groups increase the number of nonbridging oxygens from two (phosphoryl) to three (N-acylsulfonamidyl) or four (sulfonimidyl). Six such isosteres were found to be more potent inhibitors of catalysis by bovine pancreatic RNase A than are parent compounds containing phosphoryl groups. The atomic structures of two RNase A.N-acylsulfonamide complexes were determined at high resolution by X-ray crystallography. The N-acylsulfonamidyl groups were observed to form more hydrogen bonds with active site residues than did the phosphoryl groups in analogous complexes. These data encourage the further development and use of N-acylsulfonamides and sulfonimides as antagonists of nucleic acid-binding proteins.
Functional and structural analyses of N-acylsulfonamide-linked dinucleoside inhibitors of RNase A.,Thiyagarajan N, Smith BD, Raines RT, Acharya KR FEBS J. 2010 Dec 4. doi: 10.1111/j.1742-4658.2010.07976.x. PMID:21205197[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
- ↑ Thiyagarajan N, Smith BD, Raines RT, Acharya KR. Functional and structural analyses of N-acylsulfonamide-linked dinucleoside inhibitors of RNase A. FEBS J. 2010 Dec 4. doi: 10.1111/j.1742-4658.2010.07976.x. PMID:21205197 doi:10.1111/j.1742-4658.2010.07976.x
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