» Articles » PMID: 39633021

BioDolphin As a Comprehensive Database of Lipid-protein Binding Interactions

Overview
Journal Commun Chem
Publisher Springer Nature
Specialty Chemistry
Date 2024 Dec 5
PMID 39633021
Authors
Affiliations
Soon will be listed here.
Abstract

Lipid-protein interactions are crucial for virtually all biological processes in living cells. However, existing structural databases focusing on these interactions are limited to integral membrane proteins. A systematic understanding of diverse lipid-protein interactions also encompassing lipid-anchored, peripheral membrane and soluble lipid binding proteins remains to be elucidated. To address this gap and facilitate the research of universal lipid-protein assemblies, we developed BioDolphin - a curated database with over 127,000 lipid-protein interactions. BioDolphin provides comprehensive annotations, including protein functions, protein families, lipid classifications, lipid-protein binding affinities, membrane association type, and atomic structures. Accessible via a publicly available web server ( www.biodolphin.chemistry.gatech.edu ), users can efficiently search for lipid-protein interactions using a wide range of options and download datasets of interest. Additionally, BioDolphin features interactive 3D visualization of each lipid-protein complex, facilitating the exploration of structure-function relationships. BioDolphin also includes detailed information on atomic-level intermolecular interactions between lipids and proteins that enable large scale analysis of both paired complexes and larger assemblies. As an open-source resource, BioDolphin enables global analysis of lipid-protein interactions and supports data-driven approaches for developing predictive machine learning algorithms for lipid-protein binding affinity and structures.

References
1.
Rose Y, Duarte J, Lowe R, Segura J, Bi C, Bhikadiya C . RCSB Protein Data Bank: Architectural Advances Towards Integrated Searching and Efficient Access to Macromolecular Structure Data from the PDB Archive. J Mol Biol. 2020; 433(11):166704. PMC: 9093041. DOI: 10.1016/j.jmb.2020.11.003. View

2.
Moody D, Suliman S . CD1: From Molecules to Diseases. F1000Res. 2017; 6:1909. PMC: 5664979. DOI: 10.12688/f1000research.12178.1. View

3.
Bittrich S, Bhikadiya C, Bi C, Chao H, Duarte J, Dutta S . RCSB Protein Data Bank: Efficient Searching and Simultaneous Access to One Million Computed Structure Models Alongside the PDB Structures Enabled by Architectural Advances. J Mol Biol. 2023; 435(14):167994. PMC: 11514064. DOI: 10.1016/j.jmb.2023.167994. View

4.
Paysan-Lafosse T, Blum M, Chuguransky S, Grego T, Pinto B, Salazar G . InterPro in 2022. Nucleic Acids Res. 2022; 51(D1):D418-D427. PMC: 9825450. DOI: 10.1093/nar/gkac993. View

5.
Scott J, Pawson T . Cell signaling in space and time: where proteins come together and when they're apart. Science. 2009; 326(5957):1220-4. PMC: 3041271. DOI: 10.1126/science.1175668. View