Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans

Small leucine rich repeat proteoglycans (SLRPs) are a group of active components of the extracellular matrix in all tissues. SLRPs bind to collagens and regulate collagen fibril growth and fibril organization. SLRPs also interact with various cytokines and extracellular compounds, which lead to various biological functions such cell adhesion and signaling, proliferation, and differentiation. Mutations in SLRP genes are associated with human diseases. Now crystal structures of five SLRPs are available. We describe some features of amino acid sequence and structures of SLRPs. We also review ligand interactions and then discuss the interaction surfaces. Furthermore, we map mutations associated with human diseases and discuss possible effects on structures by the mutations.

Automated summary

Small leucine rich repeat proteoglycans (SLRPs) play crucial roles in the extracellular matrix by binding to collagens and interacting with cytokines, affecting various biological functions in cells. Mutations in SLRP genes are linked to human diseases, and investigating the effects of these mutations on structures can provide insights into disease mechanisms.