1jvt: Difference between revisions

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[[Image:1jvt.~~gif~~|left|200px]]

[[Image:1jvt.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE FORM)~~'''~~

===CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE FORM)===

~~==Overview==~~

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~~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.

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==About this Structure==

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[[Category: Protein dynamic]]

[[Category: Protein structure-function]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 21:59:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 21:01:55 2008''

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-[[Image:1jvt.gif|left|200px]]
+{{Seed}}
+[[Image:1jvt.png|left|200px]]
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 {{STRUCTURE_1jvt|  PDB=1jvt  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE FORM)'''
+===CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE 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==
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 [[Category: Protein dynamic]]
 [[Category: Protein structure-function]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:59:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 21:01:55 2008''