A Dual Leucine-rich Repeat in Proteins from the Eukaryotic SAR Group.

Background: Leucine-rich repeats (LRRs) occurring in tandem are 20-29 amino acids long. Eleven LRR types have been recognized; they include plant-specific (PS) type with the consensus of LxxLxLxxNxL SGxIPxxIxxLxx of 24 residues and SDS22-like type with the consensus of LxxLxLxxNxL xxIxxIxxLxx of 22 residues.

Objective: A viral LRR protein in metagenome data indicated that most of the LRRs (5/6 = 0.

Numerous variants of leucine rich repeats in proteins from nucleo-cytoplasmic large DNA viruses.

Leucine rich repeats (LRRs) occurring in tandem are 20-29 amino acids long. Eleven LRR types have been recognized. Sequence features of LRRs from viruses were investigated using over 600 LRR proteins from 89 species.

Withdrawal Notice: Novel Sequence Features of Leucine-rich Repeats in Proteins from Nucleocytoplasmic Large DNA Viruses.

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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.

A crucial residue in the hydrophobic core of the solenoid structure of leucine rich repeats.

Leucine rich repeats (LRRs) with 20-30 residues form a super helix arrangement. Individual LRRs are separated into a highly conserved segment with a highly conserved (HCS) and a variable segment (VS). In LRRs short β-strands in HCS stack in parallel, while VS adopts various secondary structures.