Structural changes in glycogen phosphorylase induced by phosphorylation.
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...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1988
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| _version_ | 1826266028289556480 |
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| author | Sprang, SR Acharya, K Goldsmith, E Stuart, D Varvill, K Fletterick, R Madsen, N Johnson, L |
| author_facet | Sprang, SR Acharya, K Goldsmith, E Stuart, D Varvill, K Fletterick, R Madsen, N Johnson, L |
| author_sort | Sprang, SR |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T20:32:42Z |
| format | Journal article |
| id | oxford-uuid:3196c375-2ef6-4bde-bd3a-4fdce6ffe9c6 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:32:42Z |
| publishDate | 1988 |
| record_format | dspace |
| spelling | oxford-uuid:3196c375-2ef6-4bde-bd3a-4fdce6ffe9c62022-03-26T13:08:55ZStructural changes in glycogen phosphorylase induced by phosphorylation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3196c375-2ef6-4bde-bd3a-4fdce6ffe9c6EnglishSymplectic Elements at Oxford1988Sprang, SRAcharya, KGoldsmith, EStuart, DVarvill, KFletterick, RMadsen, NJohnson, LA 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. |
| spellingShingle | Sprang, SR Acharya, K Goldsmith, E Stuart, D Varvill, K Fletterick, R Madsen, N Johnson, L Structural changes in glycogen phosphorylase induced by phosphorylation. |
| title | Structural changes in glycogen phosphorylase induced by phosphorylation. |
| title_full | Structural changes in glycogen phosphorylase induced by phosphorylation. |
| title_fullStr | Structural changes in glycogen phosphorylase induced by phosphorylation. |
| title_full_unstemmed | Structural changes in glycogen phosphorylase induced by phosphorylation. |
| title_short | Structural changes in glycogen phosphorylase induced by phosphorylation. |
| title_sort | structural changes in glycogen phosphorylase induced by phosphorylation |
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