2a7o

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(New page: 200px<br /> <applet load="2a7o" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a7o" /> '''Solution Structure of the hSet2/HYPB SRI do...)
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'''Solution Structure of the hSet2/HYPB SRI domain'''<br />
'''Solution Structure of the hSet2/HYPB SRI domain'''<br />
==Overview==
==Overview==
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The phosphorylation state of the C-terminal repeat domain (CTD) of the, largest subunit of RNA polymerase II changes as polymerase transcribes a, gene, and the distinct forms of the phospho-CTD (PCTD) recruit different, nuclear factors to elongating polymerase. The Set2 histone, methyltransferase from yeast was recently shown to bind the PCTD of, elongating RNA polymerase II by means of a novel domain termed the, Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure, of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned, three-helix bundle distinctly different from other structurally, characterized PCTD-interacting domains. NMR titration experiments mapped, the binding surface of the hSRI domain to helices 1 and 2, and Biacore, binding studies showed that the domain binds preferably to [Ser-2 +, Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats., Point-mutagenesis studies identified five residues critical for PCTD, binding. In view of the differential effects of these point mutations on, binding to different CTD phosphopeptides, we propose a model for the hSRI, domain interaction with the PCTD.
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The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from yeast was recently shown to bind the PCTD of elongating RNA polymerase II by means of a novel domain termed the Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other structurally characterized PCTD-interacting domains. NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats. Point-mutagenesis studies identified five residues critical for PCTD binding. In view of the differential effects of these point mutations on binding to different CTD phosphopeptides, we propose a model for the hSRI domain interaction with the PCTD.
==About this Structure==
==About this Structure==
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2A7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A7O OCA].
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2A7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=2A7O OCA].
==Reference==
==Reference==
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[[Category: Guan, Z.]]
[[Category: Guan, Z.]]
[[Category: Li, M.]]
[[Category: Li, M.]]
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[[Category: Phatnani, H.P.]]
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[[Category: Phatnani, H P.]]
[[Category: Sage, H.]]
[[Category: Sage, H.]]
[[Category: Zhou, P.]]
[[Category: Zhou, P.]]
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[[Category: sri domain]]
[[Category: sri domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:47:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:31 2008''

Revision as of 14:24, 21 February 2008

Image:2a7o.gif

2a7o

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Solution Structure of the hSet2/HYPB SRI domain

Overview

The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from yeast was recently shown to bind the PCTD of elongating RNA polymerase II by means of a novel domain termed the Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other structurally characterized PCTD-interacting domains. NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats. Point-mutagenesis studies identified five residues critical for PCTD binding. In view of the differential effects of these point mutations on binding to different CTD phosphopeptides, we propose a model for the hSRI domain interaction with the PCTD.

About this Structure

2A7O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1., Li M, Phatnani HP, Guan Z, Sage H, Greenleaf AL, Zhou P, Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17636-41. Epub 2005 Nov 28. PMID:16314571

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