کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5528488 | 1547999 | 2017 | 11 صفحه PDF | دانلود رایگان |
- The crystal structures of fibromodulin and chondroadherin have been determined.
- Fibromodulin and chondroadherin are monomeric in solution.
- Chondroadherin binds to a unique site in type II collagen that contains the sequence GAOGPSGFQGLOGPOGPO (O, hydroxyproline).
- In collagen fibres, the chondroadherin binding site is adjacent to the cross-linking site, KGHR.
The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~ 2.2 à 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.
Journal: Matrix Biology - Volume 63, November 2017, Pages 106-116