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

Biochim Biophys Acta Proteins Proteom. 2021 Jun;1869(6):140631. doi: 10.1016/j.bbapap.2021.140631. Epub 2021 Feb 22.

Abstract

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. Among eleven classes recognized, only RI-like, Cysteine-containing (CC), and GALA classes adopt an α-helix. However, the repeat unit lengths are usually different from each other. We performed some analyses based on the atomic coordinates in the known LRR structures. In the VS consensuses of the three classes, position 8 in the VS part is, in common, occupied by conserved aliphatic residue adopting an α-helix. This aliphatic residue is near to the two conserved hydrophobic residues at position 4 (in the center of β-strands) in two adjacent HCS parts. The conserved aliphatic residue plays a crucial role to preserve two parallel β-strands.

Keywords: Hydrophobic core; Leucine rich repeat; Residue interaction network; Robustness; Super α ⎼ loop ⎼ β structure; β-Stralp ⎼ α-helix ⎼ loop ⎼ β-strand motif.