A PARALLEL 3 STRANDED ALPHA-HELICAL BUNDLE AT THE NUCLEATION SITE OF COLLAGEN TRIPLE-HELIX FORMATION
A PARALLEL 3 STRANDED ALPHA-HELICAL BUNDLE AT THE NUCLEATION SITE OF COLLAGEN TRIPLE-HELIX FORMATION
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DOI：
10.1016/0014-5793(94)00383-1
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发表时间：
1994-05-16
期刊：
影响因子：
3.5
通讯作者：
REID, KBM
中科院分区：
文献类型：
--
作者：
HOPPE, HJ;BARLOW, PN;REID, KBM
35个氨基酸的短延伸被鉴定为负责肺表面活性蛋白D的三条相同多肽链的紧密平行缔合和三聚化的结构基序，所述肺表面活性蛋白D包含胶原区域和C型凝集素结构域。该“颈区”位于胶原序列折叠成交错三螺旋的成核位点处，并且通过CD、NMR和重组肽的交联显示，其由非交错且极强的非共价缔合的三链平行α-螺旋束组成。三条多肽链之间的这种类型的关联可能代表紧接在胶原蛋白的三螺旋区的C末端之后的共同结构特征。
A short stretch of 35 amino acids is identified as the structural motif responsible for the tight parallel association and trimerization of the three identical polypeptide chains of lung surfactant protein D, which contains both collagen regions and C-type lectin domains. This 'neck-region' is located at the nucleation site at which the collagenous sequences fold into a staggered triple-helix and is shown, by CD, NMR, and cross-linking of recombinant peptides, to consist of a triple-stranded parallel cc-helical bundle in a non-staggered, and extremely strong, non-covalent association. This type of association between three polypeptide chains may represent a common structural feature immediately following the C-terminal end of the triple-helical region of collagenous proteins.