9gpb: Difference between revisions

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[[Image:9gpb.gif|left|200px]]
{{Seed}}
[[Image:9gpb.png|left|200px]]


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{{STRUCTURE_9gpb|  PDB=9gpb  |  SCENE=  }}  
{{STRUCTURE_9gpb|  PDB=9gpb  |  SCENE=  }}  


'''THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE'''
===THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE===




==Overview==
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The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 A resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry of two helices linking each site with the subunit interface. Activation by AMP or by phosphorylation results in a quaternary conformational change that switches these two helices into the R-state conformation.
The line below this paragraph, {{ABSTRACT_PUBMED_2770867}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 2770867 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2770867}}


==About this Structure==
==About this Structure==
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[[Category: Johnson, L N.]]
[[Category: Johnson, L N.]]
[[Category: Glycogen phosphorylase]]
[[Category: Glycogen phosphorylase]]
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