- 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
- Publisher copy:
- 10.1038/336215a0
-
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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
- Copyright date:
- 1988
Journal article
Structural changes in glycogen phosphorylase induced by phosphorylation.
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