This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1o0o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1o0o.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1o0o.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1o0o| PDB=1o0o | SCENE= }}
{{STRUCTURE_1o0o| PDB=1o0o | SCENE= }}
-
'''Ribonuclease A in complex with adenosine-2',5'-diphosphate'''
+
===Ribonuclease A in complex with adenosine-2',5'-diphosphate===
-
==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 03:13:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:59:01 2008''

Revision as of 19:59, 27 July 2008

Image:1o0o.png

Template:STRUCTURE 1o0o

Ribonuclease A in complex with adenosine-2',5'-diphosphate

Template:ABSTRACT PUBMED 14573867

About this Structure

1O0O 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 Sun Jul 27 22:59:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o0o"
Personal tools