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与STAT6反式激活结构域的LXXLL基序结合的NCoA-1/SRC-1 PAS-B结构域的结晶及初步晶体学研究。

Crystallization and preliminary crystallographic studies of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain.

作者信息

Razeto Adelia, Pfitzner Edith, Becker Stefan

机构信息

Department for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen, Germany.

出版信息

Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):550-2. doi: 10.1107/S0907444903029378. Epub 2004 Feb 25.

DOI:10.1107/S0907444903029378
PMID:14993689
Abstract

Signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 (IL-4) by direct interaction with coactivators. Among them, NCoA-1, a member of the p160/steroid receptor coactivator (SRC) family, has been found to bind to STAT6 with the region B of its putative Per-Arnt-Sim (PAS) domain. STAT6 interacts specifically with NCoA-1 via an LXXLL motif in its transactivation domain. Crystals of the NCoA-1(257-385) domain in complex with the STAT6(794-814) LXXLL motif were obtained in two hexagonal space groups. The crystals in space group P6(1), with unit-cell parameters a = 61.7, b = 61.7, c = 146.5 A, alpha = beta = 90, gamma = 120 degrees, diffract to 2.8 A at a home source. Crystals belonging to space group P6(2), with unit-cell parameters a = 62.0, b = 62.0, c = 73.6 A, alpha = beta = 90, gamma = 120 degrees, diffract to 1.8 A at a synchrotron source.

摘要

信号转导子和转录激活子6(STAT6)通过与共激活因子直接相互作用来调节对白介素-4(IL-4)的转录激活。其中,p160/类固醇受体共激活因子(SRC)家族成员NCoA-1已被发现通过其假定的Per-Arnt-Sim(PAS)结构域的B区域与STAT6结合。STAT6通过其反式激活结构域中的LXXLL基序与NCoA-1特异性相互作用。NCoA-1(257-385)结构域与STAT6(794-814)LXXLL基序复合物的晶体在两个六方空间群中获得。空间群为P6(1)的晶体,其晶胞参数a = 61.7,b = 61.7,c = 146.5 Å,α = β = 90,γ = 120°,在家庭光源下衍射至2.8 Å。属于空间群P6(2)的晶体,其晶胞参数a = 62.0,b = 62.0,c = 73.6 Å,α = β = 90,γ = 120°,在同步辐射光源下衍射至1.8 Å。

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