Molecular packing in type I collagen fibrils. A model with neighbouring collagen molecules aligned in axial register.
A detailed stereochemical analysis of intermolecular interactions of collagens made with molecular models and summarized experimental data resulted in a new three-dimensional structural model for collagen fibrils. In this model collagen molecules aligned in axial register form a bunch. The bunches are aligned head to tail and penetrate by 300 A into each other, forming microfibrils; these in turn assemble into fibrils. The new model differs from all the others in that its characteristic axial regularity, with a period of 670 A, results from staggering of the adjacent microfibrils formed by unstaggered molecules rather than from the axial staggering of neighbouring collagen molecules.
Kajava
A V
AV
Institute of Protein Research, Academy of Sciences of the U.S.S.R., Moscow.
D000818:Animals; D003094:Collagen / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D051381:Rats; D013623:Tail / Q000737:chemistry; D013710:Tendons / Q000648:ultrastructure; D014961:X-Ray Diffraction
D003094:Collagen