THE PEPTIDE-BINDING DOMAIN OF THE CHAPERONE PROTEIN HSC70 HAS AN UNUSUAL SECONDARY STRUCTURE TOPOLOGY
THE PEPTIDE-BINDING DOMAIN OF THE CHAPERONE PROTEIN HSC70 HAS AN UNUSUAL SECONDARY STRUCTURE TOPOLOGY
复制标题
DOI：
10.1021/bi00019a001
复制
发表时间：
1995-05-16
期刊：
影响因子：
2.9
通讯作者：
ZUIDERWEG, ERP
中科院分区：
文献类型：
--
作者：
MORSHAUSER, RC;WANG, H;ZUIDERWEG, ERP
现代NMR方法用于确定溶液中伴侣蛋白Hsc 70的18 kDa肽结合结构域的二级结构拓扑。这份报告构成了第一个实验构象信息，这个重要的结构域的类Hsp 70蛋白。该结构域由两个四链反平行β-折叠和一个单一的α-螺旋组成。拓扑结构不类似于在主要组织相容性复合体的人白细胞抗原（HLA）蛋白中观察到的拓扑结构。这是重要的，因为这种相似性是基于有限的氨基酸同源性、二级结构预测和相关功能预测的。此外，据我们所知，在Hsc 70中鉴定的确切的曲折型β折叠拓扑结构在任何其他已知的蛋白质结构中都没有观察到。
Modern NMR methods were used to determine the secondary structure topology of the 18 kDa peptide binding domain of the chaperone protein Hsc70 in solution. This report constitutes the first experimental conformational information on this important domain of the class of Hsp70 proteins. The domain consists of two four-stranded antiparallel beta-sheets and a single alpha-helix. The topology does not resemble at all the topology observed in the human leukocyte antigen (HLA) proteins of the major histocompatibility complex. This is significant because such resemblance was predicted on the basis of limited amino acid homology, secondary structure prediction, and related function. Moreover, the exact meander-type beta-sheet topology identified in Hsc70 has to our best knowledge not been observed in any other known protein structure.