1kgd: Difference between revisions

Line 4:

==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.

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==

Line 23:

[[Category: maguk]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:13:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:54 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 23: / Line 23: @@
 [[Category: maguk]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:13:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:54 2008''