Literature DB >> 12121646

The 1.1 A crystal structure of human TGF-beta type II receptor ligand binding domain.

Christian C Boesen1, Sergei Radaev, Shawn A Motyka, Apisit Patamawenu, Peter D Sun.   

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.

Entities:  

Mesh：

Substances：

Year:  2002        PMID： 12121646     DOI： 10.1016/s0969-2126(02)00780-3

Source DB:  PubMed          Journal:  Structure        ISSN： 0969-2126            Impact factor:   5.006


  15 in total

1.  Sequential resonance assignments of the extracellular domain of the human TGFbeta type II receptor in complex with monomeric TGFbeta3.

Authors:  Udayar Ilangovan; Shashank Deep; Cynthia S Hinck; Andrew P Hinck
Journal:  J Biomol NMR       Date:  2004-05       Impact factor: 2.835

2.  Peptide ligands that use a novel binding site to target both TGF-β receptors.

Authors:  Lingyin Li; Brendan P Orner; Tao Huang; Andrew P Hinck; Laura L Kiessling
Journal:  Mol Biosyst       Date:  2010-10-04

Review 3.  Structural Biology and Evolution of the TGF-β Family.

Authors:  Andrew P Hinck; Thomas D Mueller; Timothy A Springer
Journal:  Cold Spring Harb Perspect Biol       Date:  2016-12-01       Impact factor: 10.005

4.  Structural biology of the TGFβ family.

Authors:  Erich J Goebel; Kaitlin N Hart; Jason C McCoy; Thomas B Thompson
Journal:  Exp Biol Med (Maywood)       Date:  2019-10-09

Review 5.  Design of growth factor sequestering biomaterials.

Authors:  David G Belair; Ngoc Nhi Le; William L Murphy
Journal:  Chem Commun (Camb)       Date:  2014-09-03       Impact factor: 6.222

Review 6.  Structure-guided engineering of TGF-βs for the development of novel inhibitors and probing mechanism.

Authors:  Andrew P Hinck
Journal:  Bioorg Med Chem       Date:  2018-07-07       Impact factor: 3.641

7.  The non-detergent sulfobetaine-201 acts as a pharmacological chaperone to promote folding and crystallization of the type II TGF-β receptor extracellular domain.

Authors:  Kittikhun Wangkanont; Katrina T Forest; Laura L Kiessling
Journal:  Protein Expr Purif       Date:  2015-06-11       Impact factor: 1.650

8.  A host-guest relationship in bone morphogenetic protein receptor-II defines specificity in ligand-receptor recognition.

Authors:  Lee-Chuan C Yeh; Wilfredo E Falcon; Andrea Garces; J Ching Lee; John C Lee
Journal:  Biochemistry       Date:  2012-08-23       Impact factor: 3.162

Review 9.  Regulation of TGF-beta signalling by protein phosphatases.

Authors:  Ting Liu; Xin-Hua Feng
Journal:  Biochem J       Date:  2010-09-01       Impact factor: 3.857

10.  An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.

Authors:  Sun Kyung Kim; Lindsey Barron; Cynthia S Hinck; Elyse M Petrunak; Kristin E Cano; Avinash Thangirala; Brian Iskra; Molly Brothers; Machell Vonberg; Belinda Leal; Blair Richter; Ravindra Kodali; Alexander B Taylor; Shoucheng Du; Christopher O Barnes; Traian Sulea; Guillermo Calero; P John Hart; Matthew J Hart; Borries Demeler; Andrew P Hinck
Journal:  J Biol Chem       Date:  2017-02-22       Impact factor: 5.157
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.