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Article

The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Aug 2009

Tan Kemin, Duquette Mark, Joachimiak Andrzej, Lawler Jack

Abstract excerpt

Cartilage oligomeric matrix protein (COMP), or thrombospondin-5 (TSP-5), is a secreted glycoprotein that is important for growth plate organization and function. Mutations in COMP cause two skeletal dysplasias, pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1). In this study, we determined the structure of a recombinant protein that contains the last epidermal growth factor repeat, the type 3...

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Source

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Identifiers

PMID: 19276170
DOI: 10.1096/fj.08-128090
PMCID: PMC2717772

Genes

COMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding.PMID 19276170Read ↗

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Novel and recurrent mutations in the C-terminal domain of COMP cluster in two distinct regions and result in a spectrum of phenotypes within the pseudoachondroplasia -- multiple epiphyseal dysplasia disease group.Semantic proximity Read ↗

Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX.Semantic proximity Read ↗

Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats.Semantic proximity Read ↗

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