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1pyg

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{{STRUCTURE_1pyg| PDB=1pyg | SCENE= }}
{{STRUCTURE_1pyg| PDB=1pyg | SCENE= }}
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'''STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE'''
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===STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 1962195 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1962195}}
==About this Structure==
==About this Structure==
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[[Category: Sprang, S.]]
[[Category: Sprang, S.]]
[[Category: Glycogen phosphorylase]]
[[Category: Glycogen phosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:38:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:30:02 2008''

Revision as of 21:30, 28 July 2008

Image:1pyg.png

Template:STRUCTURE 1pyg

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

Template:ABSTRACT PUBMED 1962195

About this Structure

1PYG is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate., Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB, Science. 1991 Nov 29;254(5036):1367-71. PMID:1962195

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