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

Donald L. Helseth, Joseph H. Lechner, Arthur Veis*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

97 Scopus citations

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, 9N, in a unique site at the β‐turn end of the telopeptide.

Original languageEnglish (US)
Pages (from-to)3005-3014
Number of pages10
JournalBiopolymers
Volume18
Issue number12
DOIs
StatePublished - Jan 1 1979

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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