CRYSTAL-STRUCTURE AT 2.2-ANGSTROM RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN
CRYSTAL-STRUCTURE AT 2.2-ANGSTROM RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN
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DOI：
10.1016/0092-8674(94)90190-2
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发表时间：
1994-10-21
期刊：
影响因子：
64.5
通讯作者：
SIGLER, PB
中科院分区：
文献类型：
--
作者：
FERGUSON, KM;LEMMON, MA;SIGLER, PB
人动力素的Pleckstrin同源(PH)结构域的X射线晶体结构已细化到2.2 Angstrom分辨率。由两个正交的反平行的β折叠组成的七链β三明治的一角被C-末端的α螺旋封闭。在这个螺旋的对面是三个环，它们在PH结构域中变化最大。基本折叠与最近通过核磁共振确定的另外两个PH结构域非常相似，证实了PH结构域是不同的结构模块。每个已知结构的PH结构域都是静电极化的，三个可变的环形成一个带正电荷的表面。该表面包括X连锁免疫缺陷突变在BTK PH结构域中的位置，并可作为配体结合表面。
The X-ray crystal structure of the pleckstrin homology (PH) domain from human dynamin has been refined to 2.2 Angstrom resolution. A seven-stranded beta sandwich of two orthogonal antiparallel beta sheets is closed at one corner by a C-terminal alpha helix. Opposite this helix are the three loops that vary most among PH domains. The basic fold is very similar to that of two other PH domains recently determined by nuclear magnetic resonance, confirming that PH domains are distinct structural modules. Each PH domain with known structure is electrostatically polarized, with the three variable loops forming a positively charged surface. This surface includes the position of the X-linked immunodeficiency mutation in the Btk PH domain and may serve as a ligand-binding surface.