1w4p
From Proteopedia
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- | [[Image:1w4p.gif|left|200px]] | + | [[Image:1w4p.gif|left|200px]] |
- | + | ||
- | '''BINDING OF NONNATURAL 3'-NUCLEOTIDES TO RIBONUCLEASE A''' | + | {{Structure |
+ | |PDB= 1w4p |SIZE=350|CAPTION= <scene name='initialview01'>1w4p</scene>, resolution 1.69Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Um3+Binding+Site+For+Chain+B'>AC1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=UM3:2'-DEOXYURIDINE 3'-MONOPHOSPHATE'>UM3</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''BINDING OF NONNATURAL 3'-NUCLEOTIDES TO RIBONUCLEASE A''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1W4P is a [ | + | 1W4P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4P OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15670155 15670155] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] | ||
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[[Category: endonuclease]] | [[Category: endonuclease]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
- | [[Category: nonnatural 3'- | + | [[Category: nonnatural 3'-nucleotide]] |
[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
- | [[Category: rnase | + | [[Category: rnase some]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:52:07 2008'' |
Revision as of 12:52, 20 March 2008
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, resolution 1.69Å | |||||||
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Ligands: | |||||||
Activity: | Pancreatic ribonuclease, with EC number 3.1.27.5 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
BINDING OF NONNATURAL 3'-NUCLEOTIDES TO RIBONUCLEASE A
Overview
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.
About this Structure
1W4P is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
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