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  Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains

Li, Y., Spangenberg, O., Paarmann, I., Konrad, M., & Lavie, A. (2002). Structural basis for nucleotide-dependent regulation of membrane-associated guanylate kinase-like domains. Journal of Biological Chemistry, 277(6), 4159-4165. Retrieved from http://www.jbc.org/content/277/6/4159.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-94F5-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E0B9-8
Genre: Journal Article

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Li, Y.1, Author              
Spangenberg, O.1, Author              
Paarmann, I., Author
Konrad, M.2, Author              
Lavie, A., Author
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1Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society, ou_578622              
2Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612              

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 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 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.

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Language(s): eng - English
 Dates: 2002-02-08
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 277 (6) Sequence Number: - Start / End Page: 4159 - 4165 Identifier: -