Wess T J, Hammersley A P, Wess L, Miller A
Department of Biological and Molecular Sciences, University of Stirling, Stirling, FK9 4LA, United Kingdom.
J Struct Biol. 1998;122(1-2):92-100. doi: 10.1006/jsbi.1998.3991.
In this review, recent results from X-ray diffraction studies of tendon are used to develop an understanding of the molecular packing of type I collagen in tendon fibrils. These cover the definition of the unit cell as triclinic, the lateral architecture of molecular packing in a fibril and the molecular packing topology of a structure that gives good agreement with X-ray diffraction data. The proposed model is a 1D staggered left handed microfibril; the molecular orientation of the telopeptides indicates that there are interconnections between microfibrils that may explain the difficulty in isolating individual microfibrillar structures. This is the first structure that defines the absolute molecular packing of molecular segments based on X-ray diffraction data. These results are discussed in the light of direct and indirect evidence relating to molecular packing such as mineralization, natural crosslink position, and biomechanical evidence. The ability of the proposed structure to fulfill many of the structural and biochemical criteria point towards the structure providing a basis for a consensus model of collagen packing.
在本综述中，利用近期对肌腱进行X射线衍射研究的结果，来深入了解I型胶原蛋白在肌腱原纤维中的分子堆积情况。这些研究涵盖了将晶胞定义为三斜晶系、原纤维中分子堆积的横向结构以及与X射线衍射数据高度吻合的结构的分子堆积拓扑结构。所提出的模型是一维交错左旋微原纤维；端肽的分子取向表明微原纤维之间存在相互连接，这或许可以解释分离单个微原纤维结构时的困难。这是首个基于X射线衍射数据定义分子片段绝对分子堆积的结构。结合与分子堆积相关的直接和间接证据，如矿化、天然交联位置及生物力学证据，对这些结果进行了讨论。所提出的结构能够满足许多结构和生化标准，这表明该结构为胶原蛋白堆积的共识模型提供了基础。
