1M9Z

CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN

Summary for 1M9Z

• Entry DOI: 10.2210/pdb1m9z/pdb
• Related: 1KTZ
• Descriptor: TGF-BETA RECEPTOR TYPE II, GLYCEROL (3 entities in total)
• Functional Keywords: three finger toxin fold, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 12716.34

Authors

Boesen, C.C.,Radaev, S.,Motyka, S.A.,Patamawenu, A.,Sun, P.D. (deposition date: 2002-07-30, release date: 2002-09-11, Last modification date: 2024-10-16)

Primary citation

Boesen, C.C.,Radaev, S.,Motyka, S.A.,Patamawenu, A.,Sun, P.D.
THE 1.1A CRYSTAL STRUCTURE OF HUMAN TGF-BETA TYPE II RECEPTOR LIGAND BINDING DOMAIN
Structure, 10:913-919, 2002

PubMed Abstract: 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 A 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.

PubMed: 12121646
DOI: 10.1016/S0969-2126(02)00780-3

Experimental method

X-RAY DIFFRACTION (1.05 Å)