1o0f

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[[Image:1o0f.gif|left|200px]]<br /><applet load="1o0f" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1o0f.gif|left|200px]]
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caption="1o0f, resolution 1.50&Aring;" />
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'''RNASE A in complex with 3',5'-ADP'''<br />
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{{Structure
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|PDB= 1o0f |SIZE=350|CAPTION= <scene name='initialview01'>1o0f</scene>, resolution 1.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=A3P:ADENOSINE-3'-5'-DIPHOSPHATE'>A3P</scene>
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|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]
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|GENE=
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}}
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'''RNASE A in complex with 3',5'-ADP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1O0F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=A3P:'>A3P</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O0F OCA].
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1O0F 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=1O0F OCA].
==Reference==
==Reference==
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High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors., Leonidas DD, Chavali GB, Oikonomakos NG, Chrysina ED, Kosmopoulou MN, Vlassi M, Frankling C, Acharya KR, Protein Sci. 2003 Nov;12(11):2559-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14573867 14573867]
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High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors., Leonidas DD, Chavali GB, Oikonomakos NG, Chrysina ED, Kosmopoulou MN, Vlassi M, Frankling C, Acharya KR, Protein Sci. 2003 Nov;12(11):2559-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14573867 14573867]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Pancreatic ribonuclease]]
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[[Category: ribonuclease]]
[[Category: ribonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:12:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:04:04 2008''

Revision as of 11:04, 20 March 2008


PDB ID 1o0f

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands:
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Coordinates: save as pdb, mmCIF, xml



RNASE A in complex with 3',5'-ADP


Overview

The crystal structures of bovine pancreatic ribonuclease A (RNase A) in complex with 3',5'-ADP, 2',5'-ADP, 5'-ADP, U-2'-p and U-3'-p have been determined at high resolution. The structures reveal that each inhibitor binds differently in the RNase A active site by anchoring a phosphate group in subsite P1. The most potent inhibitor of all five, 5'-ADP (Ki = 1.2 microM), adopts a syn conformation (in contrast to 3',5'-ADP and 2',5'-ADP, which adopt an anti), and it is the beta- rather than the alpha-phosphate group that binds to P1. 3',5'-ADP binds with the 5'-phosphate group in P1 and the adenosine in the B2 pocket. Two different binding modes are observed in the two RNase A molecules of the asymmetric unit for 2',5'-ADP. This inhibitor binds with either the 3' or the 5' phosphate groups in subsite P1, and in each case, the adenosine binds in two different positions within the B2 subsite. The two uridilyl inhibitors bind similarly with the uridine moiety in the B1 subsite but the placement of a different phosphate group in P1 (2' versus 3') has significant implications on their potency against RNase A. Comparative structural analysis of the RNase A, eosinophil-derived neurotoxin (EDN), eosinophil cationic protein (ECP), and human angiogenin (Ang) complexes with these and other phosphonucleotide inhibitors provides a wealth of information for structure-based design of inhibitors specific for each RNase. These inhibitors could be developed to therapeutic agents that could control the biological activities of EDN, ECP, and ANG, which play key roles in human pathologies.

About this Structure

1O0F is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

High-resolution crystal structures of ribonuclease A complexed with adenylic and uridylic nucleotide inhibitors. Implications for structure-based design of ribonucleolytic inhibitors., Leonidas DD, Chavali GB, Oikonomakos NG, Chrysina ED, Kosmopoulou MN, Vlassi M, Frankling C, Acharya KR, Protein Sci. 2003 Nov;12(11):2559-74. PMID:14573867

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