1it6: Difference between revisions

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[[Image:1it6.~~gif~~|left|200px]]

[[Image:1it6.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1~~'''~~

===CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1===

~~==Overview==~~

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The ~~crystal structure of~~ the ~~catalytic subunit of~~ the ~~protein phosphatase 1~~ (~~PP1), PP1 gamma, in complex with a marine toxin, calyculin A, was determined~~ at 2.~~0 A resolution~~. The metal binding site contains the phosphate group of calyculin A and forms a tight network via the hydrophilic interactions between PP1 and calyculin A. Calyculin A is located in two of the three grooves, ~~namely, in the hydrophobic groove and the acidic groove on the molecular surface. This~~ is the ~~first observation to note that the inhibitor adopts not a pseudocyclic conformation but an extended conformation in order to form a complex with the protein~~. ~~The amino acid terminus of calyculin A contributes, in a limited manner, to the binding to PP1 gamma, which is consistent with findings from the studies of dose~~-~~inhibition analysis.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12015153}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12015153 is the PubMed ID number.

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==About this Structure==

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[[Category: Wakimoto, T.]]

[[Category: Hydrolase-inhibitor complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 20~~:23:10 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:57:36 2008''

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-[[Image:1it6.gif|left|200px]]
+{{Seed}}
+[[Image:1it6.png|left|200px]]
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 {{STRUCTURE_1it6|  PDB=1it6  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1'''
+===CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1===
-==Overview==
+<!--
-The crystal structure of the catalytic subunit of the protein phosphatase 1 (PP1), PP1 gamma, in complex with a marine toxin, calyculin A, was determined at 2.0 A resolution. The metal binding site contains the phosphate group of calyculin A and forms a tight network via the hydrophilic interactions between PP1 and calyculin A. Calyculin A is located in two of the three grooves, namely, in the hydrophobic groove and the acidic groove on the molecular surface. This is the first observation to note that the inhibitor adopts not a pseudocyclic conformation but an extended conformation in order to form a complex with the protein. The amino acid terminus of calyculin A contributes, in a limited manner, to the binding to PP1 gamma, which is consistent with findings from the studies of dose-inhibition analysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12015153}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12015153 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12015153}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Wakimoto, T.]]
 [[Category: Hydrolase-inhibitor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:23:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 13:57:36 2008''