LRRDomäne

The LRR domain, or Leucine-Rich Repeat domain, is a protein structural motif found in a wide variety of proteins across different species. It is characterized by a series of repeating amino acid sequences, typically 20-30 residues in length, rich in leucine. These repeats are often arranged in a curved, horseshoe-shaped structure.

LRR domains are known for their role in mediating protein-protein interactions. The repeating units form a flexible scaffold that can bind to other proteins, nucleic acids, or small molecules. The specific binding properties are determined by the variable amino acids within the repeats and the flanking regions of the protein. This versatility allows LRR-containing proteins to participate in diverse cellular processes, including signal transduction, immune responses, cell adhesion, and transcriptional regulation.

Many important proteins contain LRR domains. For example, Toll-like receptors (TLRs), which are crucial components of the innate immune system, possess multiple LRR repeats in their extracellular domains that recognize pathogen-associated molecular patterns. Other examples include p53, a tumor suppressor protein, and various proteins involved in muscle development and maintenance. The study of LRR domains contributes to understanding fundamental biological mechanisms and has implications for disease research and therapeutic development.