THE STRUCTURE OF CALBINDIN-D28K
THE STRUCTURE OF CALBINDIN-D28K
批准号:
6628590
负责人:
RAJIV KUMAR
金额:
$17.89万
依托单位:
依托单位国家:
美国
项目类别:
财政年份:
2001
资助国家:
美国
项目状态:
已结题
起止时间:
2001-02-15 至 2005-01-31
中文摘要
描述(改编自申请人摘要):Calbindin-D28K是一种
未知三级结构的生物必需钙结合蛋白
这是正常神经功能所必需的。这种蛋白质还扮演着一个
在肠上皮细胞钙转运中的重要作用
还有肾脏。
这项赠款申请的目标是确定第三方解决方案
钙结合蛋白-D28K在无钙和钙结合状态下的结构
高分辨率核磁共振(核磁共振)谱,以确定
随着钙含量的增加,结合会发生什么样的结构变化
从而对蛋白质的作用机制有深入的了解
蛋白质。
这项拨款申请的假设是Calbindin-D28K,一种生物学上的
必需的EF-Hand钙结合蛋白,具有独特的三级结构
它与钙结合后发生构象变化。
具体目标是:(1)获得、利用高分辨率核磁
核磁共振波谱,溶液的三级结构
无钙和钙饱和形式的钙结合蛋白-D28K。(2)至
确定钙结合时发生的顺序结构变化
至Calbindin-D28K。(3)确定删除特定名称的影响
EF-Hands in calbindin-D28K对钙结合蛋白结构和钙结合性能的影响
钙结合蛋白-D28K。
将使用的技术包括:高分辨率1H、15N和13C核
全长和突变型钙结合蛋白的磁共振波谱;
电喷雾电离质谱仪;镧系元素荧光
光谱学;以及近端和近端的内源蛋白质荧光测定
远紫外线范围。
该项目具有重要意义,因为Calbindin-D28k的三级结构
在有无钙的情况下,最初的影响是未知的
全球蛋白质结构上的钙结合仍有待确定,以及
关于蛋白质如何折叠的信息可以提供对它如何作用的洞察
在细胞内。这些发现可能会在未来的
对神经退行性疾病、小脑功能和远期的认识
海马区增强。
英文摘要
DESCRIPTION (Adapted from the Applicant's Abstract): Calbindin-D28K is a
biologically essential calcium-binding protein of unknown tertiary structure
that is required for normal neural function. The protein also plays an
important role in the transport of calcium in epithelial cells of the intestine
and kidney.
The objective of this grant application is to determine the solution tertiary
structure of calbindin-D28K in calcium-free and calcium-bound forms by use of
high resolution nuclear magnetic resonance (NMR) spectroscopy, to determine
what structural changes occur upon the binding of increasing amounts of calcium
to the protein, and to thereby gain insights into the mechanism of action of
the protein.
The hypothesis of this grant application is that calbindin-D28K, a biologically
essential, EF-hand, calcium-binding protein, has a unique tertiary structure
which undergoes conformational changes upon binding calcium.
The specific aims are: (1) To obtain, using high-resolution nuclear magnetic
resonance (NMR) spectroscopy, the solution tertiary structure of the
calcium-free and the calcium-saturated forms of calbindin-D28K. (2) To
determine the sequential structural changes which occur upon binding of calcium
to calbindin-D28K. (3) To determine the effects of deletions of specific
EF-hands in calbindin-D28K on the structure and calcium-binding properties of
calbindin-D28K.
The techniques to be used include: high resolution 1H, 15N and 13C nuclear
magnetic resonance spectroscopy of the full-length and mutant calbindins;
electrospray ionization mass spectrometry; lanthanide fluorescence
spectroscopy; and intrinsic protein fluorescence determinations in the near and
far UV-range.
The project is of significance because the tertiary structure of calbindin-D28k
in the presence and absence of calcium is unknown, the effects of initial
calcium binding on global protein structure remain to be determined, and
information on how the protein folds could provide insight into how it acts
within cells. These findings will potentially be of significance in the
understanding of neurodegenerative disorders, cerebellar function and long-term
hippocampal potentiation.
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