ROLE OF THE AMINO-TERMINAL EXTRA-HELICAL REGION OF TYPE-I COLLAGEN IN DIRECTING THE 4D OVERLAP IN FIBRILLOGENESIS
ROLE OF THE AMINO-TERMINAL EXTRA-HELICAL REGION OF TYPE-I COLLAGEN IN DIRECTING THE 4D OVERLAP IN FIBRILLOGENESIS
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DOI：
10.1002/bip.1979.360181208
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发表时间：
1979-01-01
期刊：
影响因子：
2.9
通讯作者：
VEIS, A
中科院分区：
文献类型：
--
作者：
HELSETH, DL;LECHNER, JH;VEIS, A
胶原蛋白的氨基末端末端肽。1(I)链具有高度保守的序列。该序列采用Chou-Fasman标准进行分析，并折叠。-sheet构象，包括。beta。这是预料到的。这个折叠的发夹区有利于离子和疏水分子间与α的相互作用。1(I)链残基930-938在相邻的末端重叠的分子上。这种性质的末端重叠相互作用可以指导原纤维形成的初始步骤。预测的结构还将潜在的形成交联的赖氨酸残基9N置于。β的独特位置。-末端肽的末端。
The amino-terminal telopeptide of the collagen .alpha.1(I) chain has a highly conserved sequence. This sequence was analyzed by the Chou-Fasman criteria, and a folded .beta.-sheet conformation, including a .beta.-turn, was predicted. This folded hairpin region favors both ionic and hydrophobic intermolecular interactions with .alpha.1(I) chain residues 930-938 on a neighboring, end-overlapped molecule. An end-overlap interaction of this nature could direct the initial step in fibril formation. The predicted structure also places the potential crosslink-forming lysyl residue, 9N, in a unique site at the .beta.-turn end of the telopeptide.