PEPTIDE BINDING AND RELEASE BY PROTEINS IMPLICATED AS CATALYSTS OF PROTEIN ASSEMBLY
PEPTIDE BINDING AND RELEASE BY PROTEINS IMPLICATED AS CATALYSTS OF PROTEIN ASSEMBLY
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DOI：
10.1126/science.2756425
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发表时间：
1989-07-28
期刊：
影响因子：
56.9
通讯作者：
ROTHMAN, JE
中科院分区：
文献类型：
--
作者：
FLYNN, GC;CHAPPELL, TG;ROTHMAN, JE
HSP70家族中的两个成员，hsc70和Bip，分别参与促进内质网细胞质和管腔的蛋白质折叠和组装过程。短亲水性(8至25个残基)合成肽现在已被测试为多肽链底物的可能模拟物，以帮助确定这些活性的酶基础。Bip和hsc70都有特异的多肽结合部位。多肽结合引起三磷酸腺苷的水解，随后结合多肽释放。
Two members of the hsp70 family, termed hsc70 and BiP, have been implicated in promoting protein folding and assembly processes in the cytoplasm and the lumen of the endoplasmic reticulum, respectively. Short hydrophilic (8 to 25 residues) synthetic peptides have now been tested as possible mimics of polypeptide chain substrates to help define an enzymatic basis for these activities. Both BiP and hsc70 have specific peptide binding sites. Peptide binding elicits hydrolysis of adenosine triphosphate, with the subsequent release of bound peptide.