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          Institute: MPI für biophysikalische Chemie     Collection: Ehemalige Abteilungen     Display Documents



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ID: 17112.0, MPI für biophysikalische Chemie / Ehemalige Abteilungen
Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains
Authors:Li, Y.; Spangenberg, O.; Paarmann, I.; Konrad, M.; Lavie, A.
Language:English
Date of Publication (YYYY-MM-DD):2002-02-08
Title of Journal:Journal of Biological Chemistry
Volume:277
Issue / Number:6
Start Page:4159
End Page:4165
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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 GH 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-Angstrom 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 irk hCASK upon GMP binding. These conformational changes may act to regulate hCASK-GK function in a nucleotide-dependent manner.
Comment of the Author/Creator:Date: 2002, FEB 8
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Dieter Gallwitz / 150
MPI für biophysikalische Chemie/AG Manfred Konrad
External Affiliations:Univ Illinois, Dept Biochem & Mol Biol, 1819 W Polk St,; Chicago, IL 60612 USA
Identifiers:URL:http://www.jbc.org/content/277/6/4159.full.pdf+htm...
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