1kgd
From Proteopedia
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|PDB= 1kgd |SIZE=350|CAPTION= <scene name='initialview01'>1kgd</scene>, resolution 1.314Å | |PDB= 1kgd |SIZE=350|CAPTION= <scene name='initialview01'>1kgd</scene>, resolution 1.314Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | + | |LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kgd OCA], [http://www.ebi.ac.uk/pdbsum/1kgd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kgd RCSB]</span> | ||
}} | }} | ||
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[[Category: Paarmann, I.]] | [[Category: Paarmann, I.]] | ||
[[Category: Spangenberg, O.]] | [[Category: Spangenberg, O.]] | ||
| - | [[Category: FMT]] | ||
[[Category: cask]] | [[Category: cask]] | ||
[[Category: guanylate kinase like domain]] | [[Category: guanylate kinase like domain]] | ||
[[Category: maguk]] | [[Category: maguk]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:13 2008'' |
Revision as of 18:48, 30 March 2008
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| , resolution 1.314Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Guanylate Kinase-like Domain of Human CASK
Overview
CASK is a member of the membrane-associated guanylate kinases (MAGUK) homologs, a family of proteins that scaffold protein complexes at particular regions of the plasma membrane by utilizing multiple protein-binding domains. The GK domain of MAGUKs, which shares high similarity in amino acid sequence with yeast guanylate kinase (yGMPK), is the least characterized MAGUK domain both in structure and function. In addition to its scaffolding function, the GK domain of hCASK has been shown to be involved in transcription regulation. Here we report the crystal structure of the GK domain of human CASK (hCASK-GK) at 1.3-A resolution. The structure rationalizes the inability of the GK domain to catalyze phosphoryl transfer and strongly supports its new function as a protein-binding module. Comparison of the hCASK-GK structure with the available crystal structures of yGMPK provides insight into possible conformational changes that occur in hCASK upon GMP binding. These conformational changes may act to regulate hCASK-GK function in a nucleotide-dependent manner.
About this Structure
1KGD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains., Li Y, Spangenberg O, Paarmann I, Konrad M, Lavie A, J Biol Chem. 2002 Feb 8;277(6):4159-65. Epub 2001 Nov 29. PMID:11729206
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