5mx0
From Proteopedia
Crystal structure of human fibromodulin
Structural highlights
FunctionFMOD_HUMAN Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis (By similarity). Publication Abstract from PubMedThe small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2A 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 alpha2beta1 maps to an alpha-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. Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin.,Paracuellos P, Kalamajski S, Bonna A, Bihan D, Farndale RW, Hohenester E Matrix Biol. 2017 Feb 17. pii: S0945-053X(17)30015-X. doi:, 10.1016/j.matbio.2017.02.002. PMID:28215822[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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