Fibrillar Collagens.

Jordi Bella, David J. S. Hulmes

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

Fibrillar collagens (types I, II, III, V, XI, XXIV and XXVII) constitute a sub-group within the collagen family (of which there are 28 types in humans) whose functions are to provide three-dimensional frameworks for tissues and organs. These networks confer mechanical strength as well as signalling and organizing functions through binding to cellular receptors and other components of the extracellular matrix (ECM). Here we describe the structure and assembly of fibrillar collagens, and their procollagen precursors, from the molecular to the tissue level. We show how the structure of the collagen triple-helix is influenced by the amino acid sequence, hydrogen bonding and post-translational modifications, such as prolyl 4-hydroxylation. The numerous steps in the biosynthesis of the fibrillar collagens are reviewed with particular attention to the role of prolyl 3-hydroxylation, collagen chaperones, trimerization of procollagen chains and proteolytic maturation. The multiple steps controlling fibril assembly are then discussed with a focus on the cellular control of this process in vivo. Our current understanding of the molecular packing in collagen fibrils, from different tissues, is then summarized on the basis of data from X-ray diffraction and electron microscopy. These results provide structural insights into how collagen fibrils interact with cell receptors, other fibrillar and non-fibrillar collagens and other ECM components, as well as enzymes involved in cross-linking and degradation.
Original languageEnglish
Title of host publicationFibrous Proteins: Structures and Mechanisms
EditorsDavid A. D. Parry, John M. Squire
PublisherSpringer Nature
Pages457-490
Number of pages34
Edition1st
ISBN (Electronic)978-3-319-49674-0
ISBN (Print)978-3-319-49672-6
DOIs
Publication statusPublished - 2017

Publication series

NameSubcellular Biochemistry
PublisherSpringer
Volume82

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