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Allosteric interactions of glycogen phosphorylase b. A crystallographic study of glucose 6-phosphate and inorganic phosphate binding to di-imidate-cross-linked phosphorylase b.

Abstract:

The binding to glycogen phosphorylase b of glucose 6-phosphate and inorganic phosphate (respectively allosteric inhibitor and substrate/activator of the enzyme) were studied in the crystal at 0.3 nm (3A) resolution. Glucose 6-phosphate binds in the alpha-configuration at a site that is close to the AMP allosteric effector site at the subunit-subunit interface and promotes several conformational changes. The phosphate-binding site of the enzyme for glucose 6-phosphate involves contacts to two ...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
Journal:
Biochemical journal More from this journal
Volume:
218
Issue:
1
Pages:
45-60
Publication date:
1984-02-01
EISSN:
1470-8728
ISSN:
0264-6021
Language:
English
Keywords:
Pubs id:
pubs:17199
UUID:
uuid:e8bfda87-64cf-4052-98ff-e94e4e5b2360
Local pid:
pubs:17199
Source identifiers:
17199
Deposit date:
2012-12-19

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