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Role of the amino-terminal extrahelical region of type I collagen in directing the 4D overlap in fibrillogenesis

✍ Scribed by Donald L. Helseth Jr.; Joseph H. Lechner; Arthur Veis


Publisher
Wiley (John Wiley & Sons)
Year
1979
Tongue
English
Weight
624 KB
Volume
18
Category
Article
ISSN
0006-3525

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✦ Synopsis


Abstract

The amino‐terminal telopeptide of the collagen α1(I) chain has a highly conserved sequence. This sequence was analyzed by the Chou‐Fasman criteria, and a folded β‐sheet conformation, including a β‐turn, was predicted. This folded “hairpin” region favors both ionic and hydrophobic intermolecular interactions with α1(I) chain residues 930–938 on a neighboring, end‐overlapped molecule. An end‐overlap interaction of this nature could direct the initial step in fibril formation. The predicted structure also places the potential crosslink‐forming lysyl residue, 9^N^, in a unique site at the β‐turn end of the telopeptide.


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