Crystal Structure of a Rigid Four-Spectrin-Repeat Fragment of the Human Desmoplakin Plakin Domain

JOURNAL OF MOLECULAR BIOLOGY

卷:409

Article

Choi, Hee-Jung^1,2  Weis, William I.^1,2 

[1] Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA

[2] Stanford Univ, Sch Med, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA

关键词: desmoplakin;    spectrin repeats;    SH3 domain;   

DOI  :  10.1016/j.jmb.2011.04.046

来源: Elsevier

【 摘 要 】

The plakin protein family serves to connect cell-cell and cell-matrix adhesion molecules to the intermediate filament cytoskeleton. Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The 1056-amino-acid N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs). We determined the crystal structure of a fragment of DP, residues 175-630, consisting of four SRs and an inserted SH3 domain. The four repeats form an elongated, rigid structure. The SH3 domain is present in a loop between two helices of an SR and interacts extensively with the preceding SR in a manner that appears to limit inter-repeat flexibility. The intimate intramolecular association of the SH3 domain with the preceding SR is also observed in plectin, another plakin protein, but not in alpha-spectrin, suggesting that the SH3 domain of plakins contributes to the stability and rigidity of this subfamily of SR-containing proteins. (C) 2011 Elsevier Ltd. All rights reserved.

【 授权许可】

Free