Fibrous proteins are structural proteins characterized by elongated polypeptide conformations, repetitive sequence organization, and assembly into ordered extracellular fibrils, fibers, microfibrils, or networks. In connective-tissue biology and the genetics of connective-tissue disorders, the term principally encompasses collagen proteins and the protein constituents of elastic fibers, including tropoelastin and fibrillin-containing microfibrils. Collagens contain glycine-rich repeating sequences that support triple-helical molecular organization and the formation of tissue-specific supramolecular matrices [1][2]. Their biosynthesis includes intracellular post-translational processing, secretion of procollagen, proteolytic maturation, fibril assembly, and covalent cross-link formation [2]. Elastic fibers contain a cross-linked elastin core formed from tropoelastin and a microfibrillar scaffold composed largely of fibrillin and associated extracellular proteins [3]. The genetic and biochemical scope of fibrous proteins includes the encoding genes, domain architecture, post-translational modifications, intermolecular interactions, and matrix assembly processes that determine connective-tissue structure [2][3][4].
- collagen
- elastin
- protein glycosylation
- extracellular matrix
References
- G. N. Ramachandran; G. Kartha; Structure of Collagen. Nat. 1954, 174, 269-270, 10.1038/174269c0.
- Sylvie Ricard-Blum; The Collagen Family. Cold Spring Harb. Perspect. Biol. 2010, 3, a004978-a004978, 10.1101/cshperspect.a004978.
- Steven G. Wise; Anthony S. Weiss; Tropoelastin. Int. J. Biochem. Cell Biol. 2009, 41, 494-497, 10.1016/j.biocel.2008.03.017.
- Jaroslava Halper; Michael Kjaer. Basic Components of Connective Tissues and Extracellular Matrix: Elastin, Fibrillin, Fibulins, Fibrinogen, Fibronectin, Laminin, Tenascins and Thrombospondins; Springer Nature: Durham, NC, United States, 2013; pp. 31-47. [CrossRef]