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Additional resources for Structure and Function of Collagen Types
2C). These data support the network model. The polygonal model was based upon rotary shadowing studies of the association products of preformed dimers, similar to those shown in Fig. 2B, that had been reduced under nondenaturing condi tions. The physiological significance of these observations is, there fore, in question. , 1981). It was, however, not demonstrated that the observed structure was in fact type IV collagen. , 1984). The assumptions made were that the cross-linking site sequence Arg-His-Gly-Hyl, which has been conserved in in terstitial collagens, is also present in type IV collagen and that these particular sites are at certain positions along the molecule, thus allow ing formation of the proposed structure.
Another possible influence on fibril assembly is by control ling the time course in the removal of the amino and carboxy propep tides (Miyahara et al, 1984). In this context, type V collagen, which also belongs to the family of the fiber forming collagens, and is described in detail by Fessler and Fessler (this volume), should be mentioned. The primary structure of the carboxy propeptide, as well as of the triple-helical domain of type V collagen, is homologous to that of the types I, II, and III collagen.
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