1jvv: Difference between revisions

Revision as of 21:02, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jvv.png

Template:STRUCTURE 1jvv

CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)

Template:ABSTRACT PUBMED 11746706

About this StructureAbout this Structure

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

ReferenceReference

Reversible substrate-induced domain motions in ribonuclease A., Vitagliano L, Merlino A, Zagari A, Mazzarella L, Proteins. 2002 Jan 1;46(1):97-104. PMID:11746706

Page seeded by OCA on Tue Jul 1 21:01:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jvv.jpg|left|200px]]
+{{Seed}}
+[[Image:1jvv.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1jvv|  PDB=1jvv  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)'''
+===CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)===
-==Overview==
+<!--
-Despite the increasing number of successful determinations of complex protein structures the understanding of their dynamics properties is still rather limited. Using X-ray crystallography, we demonstrate that ribonuclease A (RNase A) undergoes significant domain motions upon ligand binding. In particular, when cytidine 2'-monophosphate binds to RNase A, the structure of the enzyme becomes more compact. Interestingly, our data also show that these structural alterations are fully reversible in the crystal state. These findings provide structural bases for the dynamic behavior of RNase A in the binding of the substrate shown by Petsko and coworkers (Rasmussen et al. Nature 1992;357:423-424). These subtle domain motions may assume functional relevance for more complex system and may play a significant role in the cooperativity of oligomeric enzymes.
+The line below this paragraph, {{ABSTRACT_PUBMED_11746706}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11746706 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11746706}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Protein dynamic]]
 [[Category: Protein structure-function]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:59:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 21:01:56 2008''