Open AccessNMR resonance assignment and structure prediction of the C-terminal domain of the microtubule end-binding protein 3
Author(s) -
Hazem Abdelkarim,
Ben Hitchinson,
Xinyan Qu,
Avik Banerjee,
Yulia Komarova,
Vadim Gaponenko
Publication year - 2020
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0232338
Subject(s) - microtubule , effector , plasma protein binding , biophysics , endoplasmic reticulum , microbiology and biotechnology , chemistry , computational biology , biology
End-binding proteins (EBs) associate with the growing microtubule plus ends to regulate microtubule dynamics as well as the interaction with intracellular structures. EB3 contributes to pathological vascular leakage through interacting with the inositol 1,4,5-trisphosphate receptor 3 (IP 3 R3), a calcium channel located at the endoplasmic reticulum membrane. The C-terminal domain of EB3 (residues 200–281) is functionally important for this interaction because it contains the effector binding sites, a prerequisite for EB3 activity and specificity. Structural data for this domain is limited. Here, we report the backbone chemical shift assignments for the human EB3 C-terminal domain and computationally explore its EB3 conformations. Backbone assignments, along with computational models, will allow future investigation of EB3 structural dynamics, interactions with effectors, and will facilitate the development of novel EB3 inhibitors.