1KGD

Crystal Structure of the Guanylate Kinase-like Domain of Human CASK

Summary for 1KGD

• Entry DOI: 10.2210/pdb1kgd/pdb
• Descriptor: PERIPHERAL PLASMA MEMBRANE CASK, FORMIC ACID (3 entities in total)
• Functional Keywords: maguk, cask, guanylate kinase like domain, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (By similarity): O14936
• Total number of polymer chains: 1
• Total formula weight: 20984.66

Authors

Li, Y.,Spangenberg, O.,Paarmann, I.,Konrad, M.,Lavie, A. (deposition date: 2001-11-26, release date: 2001-12-19, Last modification date: 2024-02-07)

Primary citation

Li, Y.,Spangenberg, O.,Paarmann, I.,Konrad, M.,Lavie, A.
Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains.
J.Biol.Chem., 277:4159-4165, 2002

PubMed Abstract: 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.

PubMed: 11729206
DOI: 10.1074/jbc.M110792200

Experimental method

X-RAY DIFFRACTION (1.314 Å)