期刊论文详细信息
FEBS Letters
Molecular characterization of a novel human PDZ domain protein with homology to INAD from Drosophila melanogaster
Flockerzi, Veit1  Philipp, Stephan1 
[1] Pharmakologisches Institut der Universität Heidelberg, Im Neuenheimer Feld 366, D-69120 Heidelberg, Germany
关键词: PDZ domain;    INAD;    GLGF repeat;    Capacitative calcium entry;    Membrane protein cluster;    DHR domain;   
DOI  :  10.1016/S0014-5793(97)00877-6
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

PDZ domains are thought to act as protein-binding modules mediating the clustering of membrane and membrane-associated proteins. The INAD protein has been shown to interact via a PDZ domain with the calcium channel TRP which contributes to capacitative calcium entry into Drosophila photoreceptor cells. We have cloned the cDNA of a human INAD-Like protein (hINADL) of 1524 amino acids in length containing at least five PDZ domains. Additionally, two truncated versions hINADL Δ304 and hINADL Δ853 were identified. hInadl transcripts of differing size are expressed in various tissues including brain, where transcripts are abundant in the cerebellum.

【 授权许可】

Unknown   

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