Advances in Leucine Rich Repeat Proteins
A special issue of Biology (ISSN 2079-7737). This special issue belongs to the section "Biophysics".
Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 255
Special Issue Editor
Special Issue Information
Dear Colleagues,
Leucine Rich Repeats (LRRs) consisting of 20–30 amino acids in length repeat 2–100 times in tandem. Individual LRRs are generally separated into a hallmark motif, a highly conserved segment (HCS) with the consensus of LxxLxLxxNxL or LxxLxLxxCxxL, and a variable segment (VS), in which “L” is Leu, Val, or Ile, “N” is Asn, “C” is Cys, and “x” is any amino acid. A variety of LRR classes or types have been recognized. Short β-strands in the repeating units stack in parallell and form a super helix arrangement (called a solenoid structure). LRRs are present in over 900,000 proteins ranging from viruses to eukaryotes. LRR proteins are involved in a variety of biological processes, including the immune response, signal transduction, cell adhesion, disease resistance, apoptosis, ubiquitin-related processes, DNA repair, recombination, transcription, RNA processing, nuclear mRNA transport, neuronal development, and collagen fibrillogenesis. Their functions are mostly expressed through protein or ligand interactions. Mutations of LRR protein genes are associated with various human diseases.
The goal of this Special Issue is to get a deep understanding of the correlations between sequence, structure, ligand interactions, and functions. We welcome all research related to the structures of LRR proteins by experimental and bioinformatics approaches. Additionally, sequence analyses and evolutionary research will be welcome. Original scientific reports, review articles, commentary, and perspective papers are accepted.
Prof. Dr. Norio Matsushima
Guest Editor
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Keywords
- ligand interaction
- oligomerization
- folding
- sequence
- mutation
- disease
- X-ray diffraction
- cryo-electron microscopy
- proteomics
- genomics
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