STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM BETA-SPECTRIN

被引：215

作者：

MACIAS, MJ ^{[1
]}

MUSACCHIO, A ^{[1
]}

PONSTINGL, H ^{[1
]}

NILGES, M ^{[1
]}

SARASTE, M ^{[1
]}

OSCHKINAT, H ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,D-69012 HEIDELBERG,GERMANY

来源：

NATURE | 1994年 / 369卷 / 6482期

关键词：

D O I：

10.1038/369675a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The 'pleckstrin homology' or PH domain is a 100-residue protein module. It is present in many kinases, different isoforms of phospholipase C, GTPase-activating proteins and nucleotide-exchange factors(1-4). Its function is not known, but many proteins that contain a PH domain interact with GTP-binding proteins(5). The PH domain in beta-adrenergic receptor kinase may be involved in binding to the beta gamma subunits of a trimeric G-protein(3,4,6,7). We report here the three-dimensional structure of the PH domain of the cytoskeletal protein spectrin using homonuclear nuclear magnetic resonance. The core of the molecule is an antiparallel beta-sheet consisting of seven strands. The C terminus is folded into a long alpha-helix, and another helix is present in one of the surface loops. The molecule is electrostatically polarized and contains a pocket which may be involved in the binding of a ligand. There is a distant relationship to the peptidyl-prolyl-cis-trans-isomerase FKBP in which this pocket is involved in the binding of the macrocyclic compound FK506 (refs 8-11).

引用

页码：675 / 677

页数：3

共 14 条

[1] 2-DIMENSIONAL SPECTROSCOPY - APPLICATION TO NUCLEAR MAGNETIC-RESONANCE [J].