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Conformational landscape of multidomain SMAD proteins
被引:15
作者:

Gomes, Tiago
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Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain

Martin-Malpartida, Pau
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Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain

Ruiz, Lidia
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Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain

Aragon, Eric
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Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain

Cordeiro, Tiago N.
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h-index: 0
机构:
Univ NOVA Lisboa, Inst Tecnol Quim & Biol Antonio Xavier ITQB, Av Republ, P-2780157 Oeiras, Portugal Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain

Macias, Maria J.
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h-index: 0
机构:
Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain
ICREA, Passeig Lluis Co 23, Barcelona 08010, Spain Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain
机构:
[1] Barcelona Inst Sci & Technol, Inst Res Biomed, Baldiri Reixac 10, Barcelona 08028, Spain
[2] Univ NOVA Lisboa, Inst Tecnol Quim & Biol Antonio Xavier ITQB, Av Republ, P-2780157 Oeiras, Portugal
[3] ICREA, Passeig Lluis Co 23, Barcelona 08010, Spain
基金:
欧盟地平线“2020”;
关键词:
Intrinsically disordered regions;
Multi-domain proteins;
SMAD;
Transcription factor;
TGF beta signaling;
INTRINSICALLY DISORDERED PROTEINS;
SMALL-ANGLE SCATTERING;
TGF-BETA RECEPTOR;
BIOLOGICAL MACROMOLECULES;
STRUCTURAL BASIS;
SECONDARY STRUCTURE;
NMR-SPECTROSCOPY;
CELL-MEMBRANE;
DYNAMICS;
DOMAINS;
D O I:
10.1016/j.csbj.2021.09.009
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:
SMAD transcription factors, the main effectors of the TGFO (transforming growth factor O) network, have a mixed architecture of globular domains and flexible linkers. Such a complicated architecture precluded the description of their full-length (FL) structure for many years. In this study, we unravel the structures of SMAD4 and SMAD2 proteins through an integrative approach combining Small-angle X-ray scattering, Nuclear Magnetic Resonance spectroscopy, X-ray, and computational modeling. We show that both proteins populate ensembles of conformations, with the globular domains tethered by disordered and flexible linkers, which defines a new dimension of regulation. The flexibility of the linkers facilitates DNA and protein binding and modulates the protein structure. Yet, SMAD4FL is monomeric, whereas SMAD2FL is in different monomer-dimer-trimer states, driven by interactions of the MH2 domains. Dimers are present regardless of the SMAD2FL activation state and concentration. Finally, we propose that SMAD2FL dimers are key building blocks for the quaternary structures of SMAD complexes. (C) 2021 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.
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页码:5210 / 5224
页数:15
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