Structural basis of polarity protein LGN in complex with its partner molecules

极性蛋白LGN与其伙伴分子复合物的结构基础

• 批准号: 21770116
• 负责人: YUZAWA Satoru
• 金额: $ 2.91万
• 依托单位: Kyushu University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Young Scientists (B)
• 财政年份: 2009
• 资助国家: 日本
• 起止时间: 2009 至 2010
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-21770116/
• 关键词: 蛋白質; シグナル伝達; 分子認識; X線結晶構造解析; 細胞極性

A complex in which LGN associates with a partner molecule, Insc, plays a crucial role in regulating cell polarity. To elucidate the interaction between LGN and Insc based on its tertiary structure, we have been carried out structural studies of LGN-Insc compelx using by X-ray crystallography. Regions of LGN-Insc interaction as a construct suitable for structural studies were identified and then we established the preparation of the complex. We performed crystallization trials on the LGN-Insc complex and obtained crystals suitable for X-ray diffraction after optimization of crystallization condition. X-ray diffraction data were collected to a resolution of 2.8 Å for crystals of the LGN-Insc complex.

LGN与伴侣分子iNSC结合的复合体在调节细胞极性方面起着至关重要的作用。为了从LGN-iNSC的三级结构上阐明LGN与iNSC之间的相互作用，我们用X射线结晶学方法对LGN-iNSC复合体的结构进行了研究。确定了适合于结构研究的LGN-iNSC相互作用区域，并建立了复合体的制备方法。我们对LGN-iNSC络合物进行了晶化实验，优化了晶化条件，得到了适合于X射线衍射的晶体。收集了晶体的X-射线衍射数据，分辨率为2.8Å。

项目成果

The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site.

• DOI: 10.1016/j.cell.2009.05.028
• 发表时间: 2009-08-07
• 期刊: Cell
• 影响因子: 64.5
• 作者: Bae JH;Lew ED;Yuzawa S;Tomé F;Lax I;Schlessinger J
• 通讯作者: Schlessinger J

Nox2活性化におけるp67^<phox>のドメイン配置と作用機構

p67^<phox>在Nox2激活中的结构域排列和作用机制

• 发表时间: 2009
• 作者: 湯澤聡;宮野佳;本坊和也;稲垣冬彦;住本英樹
• 通讯作者: 住本英樹

The domain organization of p67^<phox>, a protein required for activation of the superoxide-producing NADPH oxidase in hagocytes

p67^<phox> 的结构域组织，这是激活吞噬细胞中产生超氧化物的 NADPH 氧化酶所需的蛋白质

• 发表时间: 2009
• 作者: Yuzawa;S.;Miyano;K.;Honbou;K.;Inagaki;F.;Sumimoto;H.
• 通讯作者: H.

Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2

• DOI: 10.1016/j.bbrc.2009.04.011
• 发表时间: 2009-06-05
• 期刊: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
• 影响因子: 3.1
• 作者: Lulo, James;Yuzawa, Satoru;Schlessinger, Joseph
• 通讯作者: Schlessinger, Joseph

The domain organization of p67^<phox>, a protein required for activation of the superoxide-producing NADPH oxidase in phagocytes.

p67^<phox> 的结构域组织，这是一种在吞噬细胞中激活产生超氧化物的 NADPH 氧化酶所需的蛋白质。

• 发表时间: 2009
• 期刊: J.Innate Immun. 1
• 作者: Yuzawa;S.;Miyano;K.;Honbou;K.;Inagaki;F.;Sumimoto;H.
• 通讯作者: H.