Rippmann F, Taylor W R, Rothbard J B, Green N M
National Institute for Medical Research, Mill Hill, London, UK.
EMBO J. 1991 May;10(5):1053-9. doi: 10.1002/j.1460-2075.1991.tb08044.x.
The sequences of the peptide binding domains of 33 70 kd heat shock proteins (hsp70) have been aligned and a consensus secondary structure has been deduced. Individual members showed no significant deviation from the consensus, which showed a beta 4 alpha motif repeated twice, followed by two further helices and a terminus rich in Pro and Gly. The repeated motif could be aligned with the secondary structure of the functionally equivalent peptide binding domain of human leucocyte antigen (HLA) class I maintaining equivalent residues in structurally important positions in the two families and a model was built based on this alignment. The interaction of this domain with the ATP domain is considered. The overall model is shown to be consistent with the properties of products of chymotryptic cleavage.
已对33种70kd热休克蛋白(hsp70)的肽结合域序列进行比对,并推导了共有二级结构。各个成员与共有结构无明显偏差,共有结构显示β4α基序重复两次,接着是另外两个螺旋以及富含脯氨酸和甘氨酸的末端。该重复基序可与人白细胞抗原(HLA)I类功能等效的肽结合域的二级结构比对,在两个家族结构重要位置保持等效残基,并基于此比对构建了一个模型。还考虑了该结构域与ATP结构域的相互作用。整体模型显示与胰凝乳蛋白酶裂解产物的特性一致。