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

Norio Matsushima; Hiroki Miyashita; Robert H Kretsinger

doi:10.1007/s12079-021-00616-4

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

J Cell Commun Signal. 2021 Dec;15(4):519-531. doi: 10.1007/s12079-021-00616-4. Epub 2021 Apr 15.

Authors

Norio Matsushima^{1

2}, Hiroki Miyashita^{3

4}, Robert H Kretsinger⁵

Affiliations

¹ Division of Bioinformatics, Institute of Tandem Repeats, Noboribetsu, 059-0464, Japan. norio_irreko@outlook.jp.
² Center for Medical Education, Sapporo Medical University, Sapporo, 060-8556, Japan. norio_irreko@outlook.jp.
³ Division of Bioinformatics, Institute of Tandem Repeats, Noboribetsu, 059-0464, Japan.
⁴ Hokubu Rinsho Co., Ltd, Sapporo, 060⎼0061, Japan.
⁵ 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: Aromatic or methionine–aromatic interaction; Collagen binding; Interaction surface; Mutations; Super motif.

Publication types

Review