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2jmq

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Blanco, F.J.]]
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[[Category: Blanco, F J.]]
[[Category: Garcia, P.]]
[[Category: Garcia, P.]]
[[Category: Lopez-Hernandez, E.]]
[[Category: Lopez-Hernandez, E.]]
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[[Category: zn]]
[[Category: zn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:18:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:19 2008''

Revision as of 16:04, 21 February 2008

Image:2jmq.jpg

2jmq

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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 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

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