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Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.ORCID iD: 0000-0002-6600-9302
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2017 (English)In: Matrix Biology, ISSN 0945-053X, E-ISSN 1569-1802, Vol. 63, 106-116 p., S0945-053X(17)30015-XArticle in journal (Refereed) Published
Abstract [en]

The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2Å resolution of human fibromodulin and chondroadherin, two collagen-binding SLRPs. Their overall fold is similar to that of the prototypical SLRP, decorin, but unlike decorin neither fibromodulin nor chondroadherin forms a stable dimer. A previously identified binding site for integrin α2β1 maps to an α-helix in the C-terminal cap region of chondroadherin. Interrogation of the Collagen Toolkits revealed a unique binding site for chondroadherin in collagen II, and no binding to collagen III. A triple-helical peptide containing the sequence GAOGPSGFQGLOGPOGPO (O is hydroxyproline) forms a stable complex with chondroadherin in solution. In fibrillar collagen I and II, this sequence is aligned with the collagen cross-linking site KGHR, suggesting a role for chondroadherin in cross-linking.

Place, publisher, year, edition, pages
2017. Vol. 63, 106-116 p., S0945-053X(17)30015-X
Keyword [en]
Collagen, Leucine-rich repeat, X-ray crystallography
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:uu:diva-331664DOI: 10.1016/j.matbio.2017.02.002PubMedID: 28215822OAI: oai:DiVA.org:uu-331664DiVA: diva2:1149667
Note

De 2 första författarna delar förstaförfattarskapet.

Available from: 2017-10-16 Created: 2017-10-16 Last updated: 2017-11-10Bibliographically approved

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