STRUCTURAL MECHANISMS OF TGF-BETA SUPERFAMILY

TGF-β超家族的结构机制

• 批准号: 7597988
• 负责人: KENT A BAKER
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7597988
• 关键词: Binding; Bone Morphogenetic Proteins; Cell physiology; Cells; Cholinergic Agents; Computer Retrieval of Information on Scientific Projects Database; Data; Data Quality; Extracellular Domain; Funding; Grant; Institution; Ligand Binding; Ligands; Light; Pattern; Phosphorylation; Protein Family; Research; Research Personnel; Resolution; Resources; Signal Transduction; Source; Structure; Transforming Growth Factor beta; United States National Institutes of Health; blood glucose regulation; bone morphogenetic protein 9; cholinergic; receptor

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Bone Morphogenetic Proteins (BMPs), a subset of the Transforming Growth Factor-Beta superfamily, are involved in multiple cellular processes, including differentiation, patterning, and cell-fate determination. Signaling is induced when the BMP ligand binds to the extracellular domain of one type of receptor, enabling binding of a second type of receptor, resulting in the phosphorylation of the intracellular domain of the type I receptor. One newly identified ligand, BMP-9, has been shown to be involved in cholinergic differentiation and glucose homeostasis. We have recently collected diffraction data on crystals of BMP-9 of moderate quality at beam line 5.2.1 of the Advanced Light Source. We seek to obtain higher quality data and to extend the resolution for the BMP-9 structure. We are currently performing binding studies with the intent to crystallize BMP-9 with one of several receptor extracellular domains available to us in an effort to better characterize the interactions among binding partners of this important family of proteins.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 骨形态发生蛋白（BMP）是转化生长因子-Beta超家族的子集，参与了多种细胞过程，包括分化，模式和阳性测定。 当BMP配体与一种类型受体的细胞外结构域结合时，诱导信号传导，从而实现第二种受体的结合，从而导致I型受体的细胞内结构域的磷酸化。 一种新鉴定的配体BMP-9已显示与胆碱能分化和葡萄糖稳态有关。 我们最近在高级光源的光束线5.2.1上收集了有关中等质量BMP-9晶体的衍射数据。 我们寻求获得更高质量的数据并扩展BMP-9结构的分辨率。 目前，我们正在进行结合研究，目的是用几种受体外细胞域之一来结晶BMP-9，以便更好地表征这种重要的蛋白质家族的结合伙伴之间的相互作用。