1pyg: Difference between revisions

Line 1:

[[Image:1pyg.~~jpg~~|left|200px]]

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

<!--

Line 9:

Line 10:

~~'''~~STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE~~'''~~

===STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE===

~~==Overview==~~

<!--

The ~~three-dimensional structure of~~ the ~~activated state of glycogen phosphorylase~~ (~~GP)~~ as ~~induced by adenosine monophosphate (AMP~~) ~~has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP~~, ~~although~~ the ~~two regulatory signals function through different local structural mechanisms~~. ~~Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino~~- ~~and carboxyl~~-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.

The line below this paragraph, {{ABSTRACT_PUBMED_1962195}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 1962195 is the PubMed ID number.

-->

==About this Structure==

Line 25:

Line 29:

[[Category: Sprang, S.]]

[[Category: Glycogen phosphorylase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 05~~:38:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:30:02 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1pyg.jpg|left|200px]]
+{{Seed}}
+[[Image:1pyg.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1pyg|  PDB=1pyg  |  SCENE=  }}
-'''STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE'''
+===STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE===
-==Overview==
+<!--
-The three-dimensional structure of the activated state of glycogen phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP, although the two regulatory signals function through different local structural mechanisms. Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino- and carboxyl-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.
+The line below this paragraph, {{ABSTRACT_PUBMED_1962195}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1962195 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1962195}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Sprang, S.]]
 [[Category: Glycogen phosphorylase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:38:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:30:02 2008''