The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 Å resolution and 100 K: The role of the water structure and its contribution to binding-Reference-Cited by-同舟云学术

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The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 Å resolution and 100 K: The role of the water structure and its contribution to binding

Published:1998-04 Issue:4 Volume:7 Page:915-927
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Gregoriou Mary,Noble Martin E. M.,Watson Kimberly A.,Garman Elspeth F.,Johnson Louise N.,Krulle Thomas M.,Fuetene Carmen De La,Fleet George W.J.,Oikonomakos Nikos G.

Funder

MRC

Royal Society (MEMN

British Diabetes Association

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560070409/fullpdf

Reference49 articles.

1. The structural mechanism for glycogen phosphorylase control by phosphorylation and by AMP;Barford;J Mol Biol,1991

2. The allosteric transition of glycogen phosphorylase;Barford;Nature,1989

3. The molecular mechanism for the tetrameric association of glycogen phosphorylase promoted by protein phosphorylation;Barford;Protein Sci,1992

4. Potent inhibition of glycogen phosphorylase by a spirohydantoin of glucopyranose: First pyranose analogues of hydanlocidin;Bichard;Tetrahedron Letts,1995

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