1KGD

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

1KGD の概要

• エントリーDOI: 10.2210/pdb1kgd/pdb
• 分子名称: PERIPHERAL PLASMA MEMBRANE CASK, FORMIC ACID (3 entities in total)
• 機能のキーワード: maguk, cask, guanylate kinase like domain, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (By similarity): O14936
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20984.66

構造登録者

Li, Y.,Spangenberg, O.,Paarmann, I.,Konrad, M.,Lavie, A. (登録日: 2001-11-26, 公開日: 2001-12-19, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.314 Å)