We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1o0m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1o0m.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1o0m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1o0m| PDB=1o0m | SCENE= }}
{{STRUCTURE_1o0m| PDB=1o0m | SCENE= }}
-
'''Ribonuclease A in complex with uridine-2'-phosphate'''
+
===Ribonuclease A in complex with uridine-2'-phosphate===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14573867}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14573867 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14573867}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Ribonuclease]]
[[Category: Ribonuclease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:12:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:05:24 2008''

Revision as of 09:05, 28 July 2008

Image:1o0m.png

Template:STRUCTURE 1o0m

Ribonuclease A in complex with uridine-2'-phosphate

Template:ABSTRACT PUBMED 14573867

About this Structure

1O0M 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

Page seeded by OCA on Mon Jul 28 12:05:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o0m"
Personal tools