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2jmq
From Proteopedia
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(New page: 200px<br /> <applet load="2jmq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jmq" /> '''Plant Homeodomain Finger of the tumour supp...)
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Revision as of 20:50, 12 November 2007
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Plant Homeodomain Finger of the tumour suppressor ING4
Overview
Plant homeodomain (PHD) fingers are frequently present in proteins, involved in chromatin remodelling, and some of them bind to histones. The, family of proteins inhibitors of growth (ING) contains a PHD finger that, bind to histone-3 trimethylated at lysine 4, and those of ING1 and ING2, also act as nuclear phosphoinositide receptors. We have determined the, structure of ING4 PHD, and characterised its binding to phosphoinositides, and histone methylated tails. In contrast to ING2, ING4 is not a, phosphoinositide receptor and binds with similar affinity to the different, methylation states of histone-3 at lysine 4.
About this Structure
2JMQ is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4., Palacios A, Garcia P, Padro D, Lopez-Hernandez E, Martin I, Blanco FJ, FEBS Lett. 2006 Dec 22;580(30):6903-8. Epub 2006 Nov 30. PMID:17157298
Page seeded by OCA on Mon Nov 12 22:56:35 2007
Categories: Homo sapiens | Single protein | Blanco, F.J. | Garcia, P. | Lopez-Hernandez, E. | Padro, D. | Palacios, A. | ZN | Phd | Zn
