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| {{STRUCTURE_1kgd| PDB=1kgd | SCENE= }} | | {{STRUCTURE_1kgd| PDB=1kgd | SCENE= }} |
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| '''Crystal Structure of the Guanylate Kinase-like Domain of Human CASK'''
| | ===Crystal Structure of the Guanylate Kinase-like Domain of Human CASK=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11729206}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11729206 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11729206}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[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 Fri May 2 22:42:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:18:20 2008'' |
