1hlf
From Proteopedia
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|PDB= 1hlf |SIZE=350|CAPTION= <scene name='initialview01'>1hlf</scene>, resolution 2.26Å | |PDB= 1hlf |SIZE=350|CAPTION= <scene name='initialview01'>1hlf</scene>, resolution 2.26Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=GL4:8,9,10-TRIHYDROXY-7-HYDROXYMETHYL-2-THIOXO-6-OXA-1,3-DIAZA-SPIRO[4.5]DECAN-4-ONE'>GL4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ggn|1GGN]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlf OCA], [http://www.ebi.ac.uk/pdbsum/1hlf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hlf RCSB]</span> | ||
}} | }} | ||
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[[Category: Szilagyi, L.]] | [[Category: Szilagyi, L.]] | ||
[[Category: Toth, B.]] | [[Category: Toth, B.]] | ||
| - | [[Category: GL4]] | ||
| - | [[Category: PLP]] | ||
[[Category: catalytic site]] | [[Category: catalytic site]] | ||
[[Category: design]] | [[Category: design]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:13 2008'' |
Revision as of 18:07, 30 March 2008
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| , resolution 2.26Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Phosphorylase, with EC number 2.4.1.1 | ||||||
| Related: | 1GGN
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BINDING OF GLUCOPYRANOSYLIDENE-SPIRO-THIOHYDANTOIN TO GLYCOGEN PHOSPHORYLASE B: KINETIC AND CRYSTALLOGRAPHIC STUD
Overview
Glucopyranosylidene spirothiohydantoin (TH) has been identified as a potential inhibitor of both muscle and liver glycogen phosphorylase b (GPb) and a (GPa) and shown to diminish liver GPa activity in vitro. Kinetic experiments reported here show that TH inhibits muscle GPb competitively with respect to both substrates phosphate (K(i)=2.3 microM) and glycogen (K(i)=2.8 microM). The structure of the GPb-TH complex has been determined at a resolution of 2.26 A and refined to a crystallographic R value of 0.193 (R(free)=0.211). The structure of GPb-TH complex reveals that the inhibitor can be accommodated in the catalytic site of T-state GPb with very little change of the tertiary structure, and provides a basis of understanding potency and specificity of the inhibitor. The glucopyranose moiety makes the standard hydrogen bonds and van der Waals contacts as observed in the glucose complex, while the rigid thiohydantoin group is in a favourable electrostatic environment and makes additional polar contacts to the protein.
About this Structure
1HLF is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Kinetic and crystallographic studies of glucopyranosylidene spirothiohydantoin binding to glycogen phosphorylase B., Oikonomakos NG, Skamnaki VT, Osz E, Szilagyi L, Somsak L, Docsa T, Toth B, Gergely P, Bioorg Med Chem. 2002 Feb;10(2):261-8. PMID:11741774
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