The 1.1 Å crystal structure of human TGF-β type II receptor ligand binding domain

被引：47

作者：

Boesen, CC

Radaev, S

Motyka, SA

Patamawenu, A

Sun, PD ^{[1
]}

机构：

[1] NIAID, Immunogenet Lab, Struct Biol Sect, NIH, Rockville, MD 20852 USA

[2] Johns Hopkins Univ, Sch Med, Baltimore, MD 21205 USA

来源：

STRUCTURE | 2002年 / 10卷 / 07期

关键词：

D O I：

10.1016/S0969-2126(02)00780-3

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：

Transforming growth factor beta (TGF-beta) is involved in a wide range of biological functions including development, carcinogenesis, and immune regulation. Here we report the 1.1 Angstrom resolution crystal structure of human TGF-beta type II receptor ectodomain (TBRII). The overall structure of TBRII is similar to that of activin type II receptor ectodomain (ActRII) and bone morphogenic protein receptor type IA (BRIA). It displays a three-finger toxin fold with fingers formed by the beta strand pairs beta1-beta2, beta3-beta4, and beta5-beta6. The first finger in the TBRII is significantly longer than in ActRII and BRIA and folds tightly between the second finger and the C terminus. Surface charge distributions and hydrophobic patches predict potential TBRII binding sites.

引用

页码：913 / 919

页数：7

共 27 条

[21] Processing of X-ray diffraction data collected in oscillation mode [J].