3ooi
From Proteopedia
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- | + | [[Image:3ooi.png|left|200px]] | |
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===Crystal Structure of Human Histone-Lysine N-methyltransferase NSD1 SET domain in Complex with S-adenosyl-L-methionine=== | ===Crystal Structure of Human Histone-Lysine N-methyltransferase NSD1 SET domain in Complex with S-adenosyl-L-methionine=== | ||
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+ | The line below this paragraph, {{ABSTRACT_PUBMED_21196496}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 21196496 is the PubMed ID number. | ||
+ | --> | ||
+ | {{ABSTRACT_PUBMED_21196496}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[3ooi]] is a 1 chain structure with 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=3OOI OCA]. | |
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:21196496</ref><references group="xtra"/> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Wang, M.]] | [[Category: Wang, M.]] | ||
[[Category: Xu, R M.]] | [[Category: Xu, R M.]] | ||
- | [[Category: Histone-lysine n-methyltransferase]] | ||
- | [[Category: S-adenosyl-l-methionine]] | ||
- | [[Category: Set domain]] | ||
- | [[Category: Transferase]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:57:09 2010'' |
Revision as of 07:26, 16 March 2011
Crystal Structure of Human Histone-Lysine N-methyltransferase NSD1 SET domain in Complex with S-adenosyl-L-methionine
Template:ABSTRACT PUBMED 21196496
About this Structure
3ooi is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Qiao Q, Li Y, Chen Z, Wang M, Reinberg D, Xu RM. The Structure of NSD1 Reveals an Autoregulatory Mechanism Underlying Histone H3K36 Methylation. J Biol Chem. 2011 Mar 11;286(10):8361-8. Epub 2010 Dec 31. PMID:21196496 doi:10.1074/jbc.M110.204115