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Article

Structural basis of homo- and heterotrimerization of collagen I.

Nature communications - 10 Mar 2017

Sharma Urvashi, Carrique Loïc, Vadon-Le Goff Sandrine, Mariano Natacha, Georges Rainier-Numa, Delolme Frederic, Koivunen Peppi, Myllyharju Johanna, Moali Catherine, Aghajari Nushin, Hulmes David J S

Abstract excerpt

Fibrillar collagen molecules are synthesized as precursors, procollagens, with large propeptide extensions. While a homotrimeric form (three α1 chains) has been reported in embryonic tissues as well as in diseases (cancer, fibrosis, genetic disorders), collagen type I usually occurs as a heterotrimer (two α1 chains and one α2 chain). Inside the cell, the role of the C-terminal propeptides is to gather together...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Genetic Vectors

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

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Source

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Identifiers

PMID: 28281531
DOI: 10.1038/ncomms14671
PMCID: PMC5353611

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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