Structural insights into the Notch-modifying glycosyltransferase Fringe
Structural insights into the Notch-modifying glycosyltransferase Fringe
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DOI：
10.1038/nsmb1144
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发表时间：
2006-10-01
影响因子：
16.8
通讯作者：
Conti, Elena
中科院分区：
文献类型：
--
作者：
Jinek, Martin;Chen, Ya-Wen;Conti, Elena
边缘蛋白是β-1，3-N-乙酰氨基葡萄糖基转移酶，可以修饰Notch受体，改变其配体结合的特异性，从而调节发育过程中的Notch信号。我们给出了与UDP和锰结合的小鼠躁狂条纹的晶体结构。该结构揭示了与识别供体底物和催化有关的氨基酸残基，以及可能与受体底物结合的口袋。这个口袋中的几个不变残基的突变会削弱体内的条纹活性。
Fringe proteins are beta 1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo.