1Q9C
Crystal Structure of the Histone domain of Son of Sevenless
Summary for 1Q9C
| Entry DOI | 10.2210/pdb1q9c/pdb |
| Descriptor | Son of sevenless protein (1 entity in total) |
| Functional Keywords | histone fold, h2a, h2b, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 9 |
| Total formula weight | 199718.26 |
| Authors | Sondermann, H.,Soisson, S.M.,Bar-Sagi, D.,Kuriyan, J. (deposition date: 2003-08-24, release date: 2003-12-09, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 14656442DOI: 10.1016/j.str.2003.10.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.21 Å) |
Structure validation
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