Why ligand cross-reactivity is high within peptide recognition domain families? A case study on human c-src SH3 domain
DOI10.1016/J.JTBI.2013.08.026zbMATH Open1411.92096OpenAlexW2029726065WikidataQ30009569 ScholiaQ30009569MaRDI QIDQ2632341FDOQ2632341
Authors: Ping He, Wei Wu, Hai-Dong Wang, Ke-Long Liao, Wei Zhang, Feng-Lin Lv, Kang Yang 
Publication date: 14 May 2019
Published in: Journal of Theoretical Biology (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1016/j.jtbi.2013.08.026
Recommendations
- Exploring the role of cation-\(\pi\) interactions in glycoproteins lipid-binding proteins and RNA-binding proteins
- Insights into the molecular mechanisms of protein-ligand interactions by molecular docking and molecular dynamics simulation: a case of oligopeptide binding protein
- Performance of protein-ligand docking with CDK4/6 inhibitors: a case study
- Unbiased protein interface prediction based on ligand diversity quantification
- A general model of multivalent binding with ligands of heterotypic subunits and multiple surface receptors
\(c\)-src SH3 domainatomic cross-nonbonded interaction analysisligand cross-reactivitypeptide recognition domain
Cited In (2)
Uses Software
This page was built for publication: Why ligand cross-reactivity is high within peptide recognition domain families? A case study on human \(c\)-src SH3 domain
Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q2632341)
