The 1.1 A crystal structure of human TGF-beta type II receptor ligand binding domain.
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.
Structural Biology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852, USA.
Christian C
CC
Boesen
Sergei
S
Radaev
Shawn A
SA
Motyka
Apisit
A
Patamawenu
Peter D
PD
Sun
D030201:Activin Receptors, Type I / Q000737:chemistry; D000595:Amino Acid Sequence; D001665:Binding Sites; D052005:Bone Morphogenetic Protein Receptors, Type I; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases; D017434:Protein Structure, Tertiary; D000077294:Receptor, Transforming Growth Factor-beta Type II; D017978:Receptors, Growth Factor; D018125:Receptors, Transforming Growth Factor beta / Q000737:chemistry*
D008024:Ligands; D017978:Receptors, Growth Factor; D018125:Receptors, Transforming Growth Factor beta; D017346:Protein Serine-Threonine Kinases; D030201:Activin Receptors, Type I; C498211:BMPR1A protein, human; D052005:Bone Morphogenetic Protein Receptors, Type I; D000077294:Receptor, Transforming Growth Factor-beta Type II