2JMJ

NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide

Summary for 2JMJ

• Entry DOI: 10.2210/pdb2jmj/pdb
• Related: 2JMI
• Descriptor: Protein YNG1, Histone H3, ZINC ION (3 entities in total)
• Functional Keywords: histone, phd, h3k4me3, complex, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: Q08465 P61830
• Total number of polymer chains: 2
• Total formula weight: 11505.79

Authors

Ilin, S.,Taverna, S.D.,Rogers, R.S.,Tanny, J.C.,Lavender, H.,Li, H.,Baker, L.,Boyle, J.,Blair, L.P.,Chait, B.T.,Patel, D.J.,Aitchison, J.D.,Tackett, A.J.,Allis, C.D. (deposition date: 2006-11-15, release date: 2007-07-03, Last modification date: 2023-12-20)

• Primary citation: Taverna, S.D.,Ilin, S.,Rogers, R.S.,Tanny, J.C.,Lavender, H.,Li, H.,Baker, L.,Boyle, J.,Blair, L.P.,Chait, B.T.,Patel, D.J.,Aitchison, J.D.,Tackett, A.J.,Allis, C.D.; Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs; Mol.Cell, 24:785-796, 2006; PubMed: 17157260; DOI: 10.1016/j.molcel.2006.10.026

Experimental method

SOLUTION NMR