1Q9C

Crystal Structure of the Histone domain of Son of Sevenless

1Q9C の概要

• エントリーDOI: 10.2210/pdb1q9c/pdb
• 分子名称: Son of sevenless protein (1 entity in total)
• 機能のキーワード: histone fold, h2a, h2b, signaling protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 199718.26

構造登録者

Sondermann, H.,Soisson, S.M.,Bar-Sagi, D.,Kuriyan, J. (登録日: 2003-08-24, 公開日: 2003-12-09, 最終更新日: 2024-10-30)

主引用文献

Sondermann, H.,Soisson, S.M.,Bar-Sagi, D.,Kuriyan, J.
Tandem Histone Folds in the Structure of the N-terminal Segment of the Ras Activator Son of Sevenless
Structure, 11:1583-1593, 2003

PubMed Abstract: The Ras activator Son of Sevenless (Sos) contains a Cdc25 homology domain, responsible for nucleotide exchange, as well as Dbl/Pleckstrin homology (DH/PH) domains. We have determined the crystal structure of the N-terminal segment of human Sos1 (residues 1-191) and show that it contains two tandem histone folds. While the N-terminal domain is monomeric in solution, its structure is surprisingly similar to that of histone dimers, with both subunits of the histone "dimer" being part of the same peptide chain. One histone fold corresponds to the region of Sos that is clearly similar in sequence to histones (residues 91-191), whereas the other is formed by residues in Sos (1-90) that are unrelated in sequence to histones. Residues that form a contiguous patch on the surface of the histone domain of Sos are conserved from C. elegans to humans, suggesting a potential role for this domain in protein-protein interactions.

PubMed: 14656442
DOI: 10.1016/j.str.2003.10.015

実験手法

X-RAY DIFFRACTION (3.21 Å)