Katz E P, David C W
Department of BioStructure and Function, University of Connecticut Health Center, Farmington 06030-3705.
J Mol Biol. 1992 Dec 5;228(3):963-9. doi: 10.1016/0022-2836(92)90878-n.
We used molecular mechanics to study the role of gly X-Y+ sequences, where X- was Asp or Glu and Y+ was Lys or Arg, in the molecular packing of type I collagen. In the minimal energy conformation of a triply stranded molecule having a coiled-coil configuration, the side-chains of these sequences segregated into two oppositely charged groupings of the forms X-Y+X- and Y+X-Y+. Groupings having the same net charge were clustered along two complementary azimuthal edges of the molecule. Intermolecular interactions, through these oppositely charged edges, align the molecules appropriately for the formation of the HHL crosslink of skin. This alignment also can account for the axial periodicity and chiral appearance of skin collagen fibrils.
我们运用分子力学研究了甘氨酸X-Y+序列（其中X-为天冬氨酸或谷氨酸，Y+为赖氨酸或精氨酸）在I型胶原蛋白分子堆积中的作用。在具有卷曲螺旋结构的三链分子的最低能量构象中，这些序列的侧链分离成X-Y+X-和Y+X-Y+两种带相反电荷的基团。具有相同净电荷的基团沿着分子的两条互补方位边缘聚集。通过这些带相反电荷的边缘进行分子间相互作用，使分子适当地排列，以形成皮肤的HHL交联。这种排列也可以解释皮肤胶原纤维的轴向周期性和手性外观。
