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Sequence features,structure, ligand interaction,and diseases in small leucine rich repeat proteoglycans
Authors:Norio Matsushima  Hiroki Miyashita  Robert H. Kretsinger
Affiliation:1.Division of Bioinformatics, Institute of Tandem Repeats, Noboribetsu, 059-0464 Japan ;2.Center for Medical Education, Sapporo Medical University, Sapporo, 060-8556 Japan ;3.Hokubu Rinsho Co., Ltd, Sapporo, 060⎼0061 Japan ;4.Department of Biology, University of Virginia, Charlottesville, VA 22904 USA
Abstract: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.
Keywords:Super motif, Aromatic or methionine–  aromatic interaction, Collagen binding, Interaction surface, Mutations
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