Cysteinome:About

Cysteine is a unique amino acid with the thiol side chain serving as an intrinsic nucleophile and often participating in various enzymatic reactions. In recent years, covalent probes or inhibitors homing at a cysteine thiol group present in the target proteins have attracted significant attention. But the lack of systematic information for proteins with targetable cysteine has hindered the design and discovery of covalent modulators of protein functions and activities. Therefore, a comprehensive database with an analysis system dedicated to proteins with targetable cysteine can be very useful. Cysteinome, the first online database that provides a rich resource for the display, search and analysis of structure, function and related annotation for proteins with targetable cysteine as well as their covalent modulators.
Cysteinome will contribute to the understanding of how protein targets is covalently modified by chemical probes homing at cysteine residue and will serve as a useful resource for the development of covalent inhibitors Cysteinome is able to provide considerably more information about proteins and ligands by hyperlinking to the particular databases, such as UniProt, KEGG, PDB and PubChem.

In Cysteinome, users could start by two ways:

1. From the Target List, it could be found that the proteins are classified by the species. During these catalogues, the “Animal” is the biggest one, which contains the targets from Human, Mouse, Rat, Bovine, some Insects and so on. Besides, in Cysteinome there are “Bacteria”, “Virus”, “Parasite” and “Plant”.
2. From the Search, users can start by searching the name and UNP ID of the protein, or the name and PubChem cid of the ligands (most of the ligands possess a PubChem cid).

Taken “Streptopain” as an example, from the entry, users could easily overview the target and get access to the other databases convenient:

Taken “Oxacillin” as the example of ligand:

We hope that Cysteinome will contribute to the understanding of how protein targets is covalently modified by chemical probes homing at cysteine residue and will serve as a useful resource for the development of covalent inhibitors.

Cysteinome is developed by Center for Molecular Medicine, School of Life Science and Biotechnology, Dalian University of Technology, China, and now maintained by College of Pharmacy, The Ohio State University, USA.

People

Sijin Wu, Ph.D.: postdocatoral researcher at College of Pharmacy, OSU.

Yongliang Yang, Ph.D.: associate professor at Center for Molecular Medicine, School of Life Science and Biotechnology, DLUT.