DETERMINANTS OF CALCIUM BINDING IN NON EF HAND PROTEINS

非 EF 手蛋白中钙结合的决定因素

• 批准号: 2696556
• 负责人: LAWRENCE Jules BERLINER
• 金额: $ 18.33万
• 依托单位: OHIO STATE UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-08-01 至 2002-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2696556
• 关键词: aminoacid; calcium binding protein; electron spin resonance spectroscopy; galactosyltransferases; lactalbumin; membrane proteins; nuclear magnetic resonance spectroscopy; protein binding; protein folding; protein sequence; protein structure function; site directed mutagenesis; stop flow technique; zinc

DESCRIPTION: Biochemists and structural biologists have learned a tremendous amount about a common group of calcium-binding proteins containing the "EF-han motif" (troponin C, parvalbumin, calmodulin, etc.) from which there is a relative wealth on information on their structures and function. However another unique group of proteins exist, the calcium-binding a-lactalbumins and lysozymes, which are "non-classical" calcium-binding proteins which have a unique and distinct coordination geometry. The overall topography and role of the cation binding loop in the calcium-binding alpha-lactalbumins has yet to b fully understood. Furthermore, the alpha-lactalbumins are unique in their high propensity to form the intermediate "molten globule" folding state. They also bind the metal ion zinc at another distinct site, which modulates the conformational properties of the calcium bound form. The aims of this project are to unravel the structural and functional properties of the calcium binding properties of this milk protein, which modifies the specificity of the enzyme galactosyl transferase in lactose biosynthesis. The specific aims of this project are to: 1. Unravel the determinants involved in calcium binding (and in the folding an structural integrity of the protein). 2. Determine which residues of the protein are buried in membranes. 3. Determine the role of the amino acids involved in zinc binding.

描述：生物化学家和结构生物学家已经学会了一个 一组常见的钙结合蛋白 含有“EF-han基序”（肌钙蛋白C、小清蛋白、钙调蛋白等） 从中有关于其结构的相对丰富的信息， 功能 然而，另一组独特的蛋白质存在， 钙结合α-乳白蛋白和溶菌酶，它们是“非经典的” 钙结合蛋白，具有独特的和独特的协调 几何 本文对阳离子结合环的总体形貌和作用进行了研究。 结合钙的α-乳白蛋白B尚未完全了解。 此外，α-乳白蛋白的独特之处在于其高倾向性， 形成中间的“熔融小球”折叠状态。 他们还绑定了 金属离子锌在另一个不同的网站，它调节构象 钙结合形式的性质。 该项目的目的是 解开钙结合的结构和功能特性， 这种牛奶蛋白的特性，它改变了牛奶的特异性， 乳糖生物合成中的半乳糖基转移酶。 该项目的具体目标是： 1. 解开参与钙结合（和折叠）的决定因素 蛋白质的结构完整性）。 2. 确定蛋白质的哪些残基埋在膜中。 3. 确定参与锌结合的氨基酸的作用。