PROTEIN-CHEMICAL CHARACTERIZATION OF 3 STRUCTURALLY DISTINCT DOMAINS ALONG THE PROTOFILAMENT UNIT OF DESMIN 10-NM FILAMENTS
PROTEIN-CHEMICAL CHARACTERIZATION OF 3 STRUCTURALLY DISTINCT DOMAINS ALONG THE PROTOFILAMENT UNIT OF DESMIN 10-NM FILAMENTS
复制标题
DOI：
10.1016/0092-8674(82)90033-2
复制
发表时间：
1982-01-01
期刊：
影响因子：
64.5
通讯作者：
WEBER, K
中科院分区：
文献类型：
--
作者：
GEISLER, N;KAUFMANN, E;WEBER, K
有限的可溶性鸡砂囊结蛋白原丝的糜蛋白酶裂解允许3个结构不同的域的表征。表面暴露的、非常碱性的氨基末端区（头部），其氨基酸序列不包括α-螺旋结构（7.5kd [千道尔顿]）可能通过. apprx的明显不同的中间结构域与球状羧基末端48个残基（尾片段）分开。330个残基。该38 kd结构域非常富含α-螺旋（≥83%），并且EM揭示了长度为500 ± 0.85的细杆。50.安..氨基酸序列数据还表明，杆域中断的非螺旋部分。一个α-螺旋阵列能够形成跨越38 kd结构域的羧基末端一半的卷曲螺旋。α-型衍射图案的10 nm的长丝产生的卷曲螺旋构象显示通过大部分，但不是全部，中间域的原丝。
Limited chymotryptic cleavage of soluble chicken gizzard desmin protofilaments allows the characterization of 3 structurally distinct domains. A surface-exposed, very basic amino-terminal region (the headpiece) with a amino acid sequence excluding .alpha.-helical organization (7.5 kd [kilodaltons]) is separated from the, perhaps, globular carboxy-terminal 48 residues (the tailpiece) by a distinctly different middle domain of .apprx. 330 residues. This 38 kd domain is very rich in .alpha.-helix (.gtoreq. 83%), and EM reveals a thin rod with a length of 500 .+-. 50 .ANG.. Amino acid sequence data also show that the rod domain is interrupted by a nonhelical portion. An .alpha.-helical array is able to form a coiled-coil spanning the carboxy-terminal half of the 38 kd domain. The .alpha.-type diffraction pattern of 10 nm filaments arises from a coiled-coil conformation displayed through most, but not all, of the middle domain of the protofilaments.