Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 May 26;15:618098. doi: 10.3389/fnins.2021.618098

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2021 Aguilera, Hümmer, Masanas, Gabau, Guitart, Jeyaprakash, Segura, Santamaria and Ruiz.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Conservation analysis and structural modeling of the R169T variant. (A) Multiple-sequence alignment showing the conservation of R169 residue in KIF1A across evolution. The alignment has been performed using HomoloGene (https://www.ncbi.nlm.nih.gov/homologene). L7, loop 7; L8, loop 8; MB1, microtubule-binding region 1. (B) Schematic representation of KIF1A bound to the alpha/beta tubular heterodimer. Insets show close-up views of (left) the electrostatic interaction mediated by KIF1A R169 with β-tubulin residues E417 and E420 and (right) the loss of electrostatic interaction caused by KIF1A R169T mutation. α-Tubulin is shown in green, β-tubulin in cyan, and KIF1A in pink. (C) Superposed structure of microtubule-bound Kinesin-1 (PDB: 3J8Y) onto microtubule-bound KIF1A (PDB: 2HXF).