BINDING-SITES INVOLVED IN THE INTERACTION OF ACTIN WITH THE N-TERMINAL REGION OF DYSTROPHIN

被引:125
作者
LEVINE, BA
MOIR, AJG
PATCHELL, VB
PERRY, SV
机构
[1] UNIV BIRMINGHAM,SCH MED,DEPT PHYSIOL,BIRMINGHAM B15 2TJ,W MIDLANDS,ENGLAND
[2] UNIV OXFORD,DEPT INORGAN CHEM,OXFORD,ENGLAND
[3] UNIV BIRMINGHAM,SCH BIOCHEM,BIRMINGHAM B15 2TT,W MIDLANDS,ENGLAND
[4] UNIV SHEFFIELD,KREBS INST BIOMOLEC RES,DEPT MOLEC BIOL & BIOTECHNOL,SHEFFIELD S10 2TN,S YORKSHIRE,ENGLAND
关键词
PROTON NMR; DYSTROPHIN; F-ACTIN; INTERACTION; ALPHA-ACTININ; BETA-SPECTRIN;
D O I
10.1016/0014-5793(92)80019-D
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Two actin-binding sites have been identified on human dystrophin by proton NMR spectroscopy of synthetic peptides corresponding to defined regions of the polypeptide sequence. These are Actin-Binding Site 1 (ABS1) located at residues 17-26 and Actin-Binding Site 2 (ABS2) in the region of residues 128-156. Using defined fragments of the actin amino acid sequence, ABS1 has been shown to bind to actin in the region represented by residues 83-117 and ABS2 to the C-terminal region represented by residues 350-375. These dystrophin-binding sites lie on the exposed domain in the actin filament.
引用
收藏
页码:44 / 48
页数:5
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