Structural assessment of OsNIP2;1 highlighted critical residues defining solute specificity and functionality of NIP class aquaporins.

ABSTRACT:

Introduction

Nodulin-26-like intrinsic proteins (NIPs) are integral membrane proteins belonging to the aquaporin family, that facilitate the transport of neutral solutes across the bilayer. The OsNIP2;1 a member of NIP-III class of aquaporins is permeable to beneficial elements like silicon and hazardous arsenic. However, the atomistic cross-talk of these molecules traversing the OsNIP2;1 channel is not well understood.

Objective

Due to the lack of genomic variation but the availability of high confidence crystal structure, this study aims to highlight structural determinants of metalloid permeation through OsNIP2;1.

Methods

The molecular simulations, combined with site-directed mutagenesis were used to probe the role of specific residues in the metalloid transport ac

SUBMITTER: Sharma Y 

PROVIDER: S-EPMC10982858 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature