Structural changes in glycogen phosphorylase induced by phosphorylation

S. R. Sprang, K. R. Acharya, E. J. Goldsmith, D. I. Stuart, K. Varvill, R. J. Fletterick, N. B. Madsen, L. N. Johnson

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)215-221
Number of pages7
JournalNature
Volume336
Issue number6196
DOIs
Publication statusPublished - 1 Jan 1988

ASJC Scopus subject areas

  • General

Cite this

Sprang, S. R., Acharya, K. R., Goldsmith, E. J., Stuart, D. I., Varvill, K., Fletterick, R. J., ... Johnson, L. N. (1988). Structural changes in glycogen phosphorylase induced by phosphorylation. Nature, 336(6196), 215-221. https://doi.org/10.1038/336215a0

Structural changes in glycogen phosphorylase induced by phosphorylation. / Sprang, S. R.; Acharya, K. R.; Goldsmith, E. J.; Stuart, D. I.; Varvill, K.; Fletterick, R. J.; Madsen, N. B.; Johnson, L. N.

In: Nature, Vol. 336, No. 6196, 01.01.1988, p. 215-221.

Research output: Contribution to journalArticle

Sprang, SR, Acharya, KR, Goldsmith, EJ, Stuart, DI, Varvill, K, Fletterick, RJ, Madsen, NB & Johnson, LN 1988, 'Structural changes in glycogen phosphorylase induced by phosphorylation', Nature, vol. 336, no. 6196, pp. 215-221. https://doi.org/10.1038/336215a0
Sprang SR, Acharya KR, Goldsmith EJ, Stuart DI, Varvill K, Fletterick RJ et al. Structural changes in glycogen phosphorylase induced by phosphorylation. Nature. 1988 Jan 1;336(6196):215-221. https://doi.org/10.1038/336215a0
Sprang, S. R. ; Acharya, K. R. ; Goldsmith, E. J. ; Stuart, D. I. ; Varvill, K. ; Fletterick, R. J. ; Madsen, N. B. ; Johnson, L. N. / Structural changes in glycogen phosphorylase induced by phosphorylation. In: Nature. 1988 ; Vol. 336, No. 6196. pp. 215-221.
@article{abf8818726cf46ce9ffd90a24036f7f5,
title = "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.",
author = "Sprang, {S. R.} and Acharya, {K. R.} and Goldsmith, {E. J.} and Stuart, {D. I.} and K. Varvill and Fletterick, {R. J.} and Madsen, {N. B.} and Johnson, {L. N.}",
year = "1988",
month = "1",
day = "1",
doi = "10.1038/336215a0",
language = "English",
volume = "336",
pages = "215--221",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6196",

}

TY - JOUR

T1 - Structural changes in glycogen phosphorylase induced by phosphorylation

AU - Sprang, S. R.

AU - Acharya, K. R.

AU - Goldsmith, E. J.

AU - Stuart, D. I.

AU - Varvill, K.

AU - Fletterick, R. J.

AU - Madsen, N. B.

AU - Johnson, L. N.

PY - 1988/1/1

Y1 - 1988/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0024290703&partnerID=8YFLogxK

U2 - 10.1038/336215a0

DO - 10.1038/336215a0

M3 - Article

VL - 336

SP - 215

EP - 221

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6196

ER -