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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 骨形态发生蛋白（BMP）是转化生长因子β超家族的一个亚类，参与多种细胞过程，包括分化、模式化和细胞命运决定。 当BMP配体结合到一种类型的受体的细胞外结构域时，信号传导被诱导，使得能够结合第二种类型的受体，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，已被证明参与胆碱能分化和葡萄糖稳态。 我们最近在高级光源的光束线5.2.1处收集了中等质量的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。 我们目前正在进行结合研究，目的是使BMP-9与我们可用的几种受体胞外结构域之一结晶，以更好地表征这个重要蛋白质家族的结合伴侣之间的相互作用。