Crystal structure of a Smad MH1 domain bound to DNA

一公 施;Yan Fel Wang;Lata Jayaraman;Haijuan Yang;Joan Massagué;Nikola P. Pavletich

Princeton University;Howard Hughes Medical Institute

发表时间:1998-9-4

期 刊:Cell

语 言:English

U R L: http://www.scopus.com/inward/record.url?scp=0032483544&partnerID=8YFLogxK

摘要

The Smad family of proteins, which are frequently targeted by tumorigenic mutations in cancer, mediate TGF-β signaling from cell membrane to nucleus. The crystal structure of a Smad3 MH1 domain bound to an optimal DNA sequence determined at 2.8 Å resolution reveals a novel DNA-binding motif. In the crystals, base-specific DNA recognition is provided exclusively by a conserved 11-residue β hairpin that is embedded in the major groove of DNA. A surface loop region, to which tumorigenic mutations map, has been identified as a functional surface important for Smad activity. This structure establishes a framework for understanding how Smad proteins may act in concert with other transcription factors in the regulation of TGF-β- responsive genes.

相关科学

生物化学、遗传学和分子生物学

文献指纹

医学与生命科学

Smad Proteins

Nucleotide Motifs

Mutation

DNA

Transcription Factors

Cell Membrane

Genes

Neoplasms

化合物

Crystal structure

DNA

Smad Proteins

Cell membranes

DNA sequences

Crystals

Genes

Transcription Factors

Proteins

被引量

期刊度量

Scopus度量

年份 CiteScore SJR SNIP
1996
1997
1998
1999 43.449 6.332
2000 36.711 5.999
2001 29.247 5.155
2002 28.027 4.956
2003 28.284 4.99
2004 25.704 5.002
2005 25.262 4.648
2006 23.831 4.889
2007 25.228 5.206
2008 25.274 5.631
2009 26.21 6.527
2010 25.629 6.426
2011 56.8 25.74 6.681
2012 55.5 25.117 6.9
2013 52.4 28.254 6.842
2014 53.9 28.505 6.776
2015 54.6 27.712 6.29
2016 53.5 27.691 6.043
2017 54.9 25.137 5.947
2018 56.2 25.976 6.769
2019 58.7 24.698 7.114
2020 62
2021

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