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Structural changes in glycogen phosphorylase induced by phosphorylation.

Abstract:
A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the surface of the dimer. The consequent structural changes at the N- and C-terminal regions lead to strengthened interactions between subunits and alter the binding sites for allosteric effectors and substrates.
Publication status:
Published

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Publisher copy:
10.1038/336215a0

Authors


Sprang, SR More by this author
Acharya, KR More by this author
Goldsmith, EJ More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Varvill, K More by this author
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Journal:
Nature
Volume:
336
Issue:
6196
Pages:
215-221
Publication date:
1988-11-05
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
URN:
uuid:3196c375-2ef6-4bde-bd3a-4fdce6ffe9c6
Source identifiers:
18414
Local pid:
pubs:18414

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