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2L3R

NMR structure of UHRF1 Tandem Tudor Domains in a complex with Histone H3 peptide

Summary for 2L3R
Entry DOI10.2210/pdb2l3r/pdb
NMR InformationBMRB: 17200
DescriptorE3 ubiquitin-protein ligase UHRF1, Histone H3 (2 entities in total)
Functional Keywordstudor domain, heterochromatin, transcriptional repression, structural genomics, structural genomics consortium, sgc, dna binding protein, dna binding protein-gene regulation complex, dna binding protein/gene regulation
Biological sourceHomo sapiens (human)
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Total number of polymer chains2
Total formula weight20174.53
Authors
Nady, N.,Lemak, A.,Fares, C.,Gutmanas, A.,Avvakumov, G.,Xue, S.,Arrowsmith, C.,Structural Genomics Consortium (SGC) (deposition date: 2010-09-21, release date: 2011-04-13, Last modification date: 2020-02-05)
Primary citationNady, N.,Lemak, A.,Walker, J.R.,Avvakumov, G.V.,Kareta, M.S.,Achour, M.,Xue, S.,Duan, S.,Allali-Hassani, A.,Zuo, X.,Wang, Y.X.,Bronner, C.,Chedin, F.,Arrowsmith, C.H.,Dhe-Paganon, S.
Recognition of Multivalent Histone States Associated with Heterochromatin by UHRF1 Protein.
J.Biol.Chem., 286:24300-24311, 2011
Cited by
PubMed: 21489993
DOI: 10.1074/jbc.M111.234104
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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