Review Article Open Access
Volume 4 | Issue 3 | DOI: https://doi.org/10.33696/Signaling.4.098

Structural Insights into Protein-Ligand Interactions of Small Leucine Rich Repeat Proteoglycans with a Large Number of Binding Partners: An Overview

  • 1Division of Bioinformatics, Institute of Tandem Repeats, Noboribetsu 059-0464, Japan
  • 2Center for Medical Education, Sapporo Medical University, Sapporo 060-8556, Japan
  • 3Hokubu Rinsho Co., Ltd, Sapporo 060-0061, Japan
  • 4Department of Physics, School of Mathematics and Natural Sciences, Mongolian National University of Education, Ulaanbaatar 210648, Mongolia
  • 5Department of Biology, University of Virginia, Charlottesville, VA 22904, USA
+ Affiliations - Affiliations

Corresponding Author

Norio Matsushima, irreko_norio@outlook.jp

Received Date: May 28, 2023

Accepted Date: July 21, 2023


Small leucine rich repeat proteoglycans (SLRPs) exist in the extracellular matrix. SLRPs contain tandem arrays of LRRs flanked by cysteine clusters at the both N- and C-termini. The extreme N- and/or C-termini contain low complexity sequences, glycosaminoglycan (GAG) chain and/or sulfated tyrosine residues in some members of SLRPs. The LRR solenoid structure may be divided into four parts consisting of a concave surface, an ascending surface, a convex surface, and a descending surface. SLRPs share many biological functions including collagen fibrillogenesis, signaling, innate immunity, and inflammation through the binding of various ligands. We undertake a comprehensive literature search of publications in order to make a list of ligands of SLRPs. We describe and discuss the interacting sites of SLRPs to binding partners. The protein-ligand interactions occur on not only the concave surface but also the ascending surface and the N- or C-terminal capping regions. In addition, the extreme N- and/or C-terminal regions with the GAG chains or sulfated tyrosine residues participate in ligand-interactions.


Small leucine rich repeat proteoglycan, Leucine rich repeat, Solenoid structure, Concave face, Ascending loop, Capping structure, Ligand interactions, Glycosamoninoglycan

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