1nw3
From Proteopedia
(New page: 200px<br /> <applet load="1nw3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nw3, resolution 2.5Å" /> '''Structure of the Cat...) |
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- | [[Image:1nw3. | + | [[Image:1nw3.jpg|left|200px]]<br /><applet load="1nw3" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1nw3" size=" | + | |
caption="1nw3, resolution 2.5Å" /> | caption="1nw3, resolution 2.5Å" /> | ||
'''Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase'''<br /> | '''Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 1NW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACT, SO4 and SAM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NW3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NW3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: histone lysine methyltransferase]] | [[Category: histone lysine methyltransferase]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:31:19 2008'' |
Revision as of 14:31, 15 February 2008
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Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase
Overview
Dot1 is an evolutionarily conserved histone methyltransferase that, methylates lysine-79 of histone H3 in the core domain. Unlike other, histone methyltransferases, Dot1 does not contain a SET domain, and it, specifically methylates nucleosomal histone H3. We have solved a 2.5 A, resolution structure of the catalytic domain of human Dot1, hDOT1L, in, complex with S-adenosyl-L-methionine (SAM). The structure reveals a unique, organization of a mainly alpha-helical N-terminal domain and a central, open alpha/beta structure, an active site consisting of a SAM binding, pocket, and a potential lysine binding channel. We also show that a, flexible, positively charged region at the C terminus of the catalytic, domain is critical for nucleosome binding and enzymatic activity. These, structural and biochemical analyses, combined with molecular modeling, provide mechanistic insights into the catalytic mechanism and nucleosomal, specificity of Dot1 proteins.
About this Structure
1NW3 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase., Min J, Feng Q, Li Z, Zhang Y, Xu RM, Cell. 2003 Mar 7;112(5):711-23. PMID:12628190
Page seeded by OCA on Fri Feb 15 16:31:19 2008
Categories: Homo sapiens | Single protein | Feng, Q. | Li, Z.H. | Min, J.R. | Xu, R.M. | Zhang, Y. | ACT | SAM | SO4 | Hdot1 | Histone lysine methyltransferase