1q9c

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(New page: 200px<br /> <applet load="1q9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q9c, resolution 3.21&Aring;" /> '''Crystal Structure o...)
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'''Crystal Structure of the Histone domain of Son of Sevenless'''<br />
'''Crystal Structure of the Histone domain of Son of Sevenless'''<br />
==Overview==
==Overview==
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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.
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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1Q9C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q9C OCA].
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1Q9C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q9C OCA].
==Reference==
==Reference==
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[[Category: Bar-Sagi, D.]]
[[Category: Bar-Sagi, D.]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
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[[Category: Soisson, S.M.]]
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[[Category: Soisson, S M.]]
[[Category: Sondermann, H.]]
[[Category: Sondermann, H.]]
[[Category: h2a]]
[[Category: h2a]]
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[[Category: histone fold]]
[[Category: histone fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:51:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:15 2008''

Revision as of 12:37, 21 February 2008


1q9c, resolution 3.21Å

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Crystal Structure of the Histone domain of Son of Sevenless

Contents

Overview

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.

Disease

Known diseases associated with this structure: Fibromatosis, gingival OMIM:[182530], Noonan syndrome 4 OMIM:[182530]

About this Structure

1Q9C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Tandem histone folds in the structure of the N-terminal segment of the ras activator Son of Sevenless., Sondermann H, Soisson SM, Bar-Sagi D, Kuriyan J, Structure. 2003 Dec;11(12):1583-93. PMID:14656442

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