Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Elucidating allosteric signal disruption in PBP2a: impact of N146K/E150K mutations on ceftaroline resistance in methicillin-resistant Staphylococcus aureus.

Journal of computer-aided molecular design - 7 Feb 2025

Jiao Fangfang, Xu Ran, Luo Qing, Li Xinkang, Tong Henry H Y, Guo Jingjing

Abstract excerpt

Ceftaroline (CFT) effectively combats methicillin-resistant Staphylococcus aureus (MRSA) by binding to the allosteric site on penicillin-binding protein 2a (PBP2a) and activating allosteric signals that remotely open the active pocket. However, the widespread clinical use of CFT has led to specific mutations, such as N146K/E150K, at the PBP2a allosteric site, which confers resistance to CFT in MRSA by disrupting...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Regulation
Share to Allosteric Site

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cephalosporins

Share to Drug Resistance, Bacterial

Share to Methicillin-Resistant Staphylococcus aureus

Share to Microbial Sensitivity Tests

Share to Molecular Dynamics Simulation

Share to Penicillin-Binding Proteins

Source

Identifiers

PMID: 39915349
DOI: 10.1007/s10822-025-00584-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Elucidating allosteric signal disruption in PBP2a: impact of N146K/E150K mutations on ceftaroline resistance in methicillin-resistant Staphylococcus aureus.PMID 39915349Read ↗

Disruption of allosteric response as an unprecedented mechanism of resistance to antibiotics.Semantic proximity Read ↗

Unraveling the mechanisms of Cefoxitin resistance in methicillin-resistant Staphylococcus aureus (MRSA): structural and molecular simulation-based insights.Semantic proximity Read ↗

Exploring PBP2a resistance in MRSA by comparison between molecular covalent docking and non-covalent dockingSemantic proximity Read ↗

How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological functionSemantic proximity Read ↗

Computer-Aided Discovery of a β-Lactam-Independent Deep-Pocket PBP2a Binding Scaffold for Combating MRSA via Pharmacophore-Guided Scaffold Hopping and Bioisosteric ReplacementSemantic proximity Read ↗

Beyond mecA: a two-tiered mechanism and regulatory rewiring drive high-level ceftaroline resistance in clinical MRSA.Semantic proximity Read ↗

Molecular Basis of Influence of A501X Mutations in Penicillin-Binding Protein 2 of Neisseria gonorrhoeae Strain 35/02 on Ceftriaxone Resistance.Semantic proximity Read ↗

Engineering dynamic gates in binding pocket of penicillin G acylase to selectively degrade bacterial signaling moleculesSemantic proximity Read ↗

A Review on Five and Six-Membered Heterocyclic Compounds Targeting the Penicillin-Binding Protein 2 (PBP2A) of Methicillin-Resistant Staphylococcus aureus (MRSA)Semantic proximity Read ↗

A Review on Five and Six-Membered Heterocyclic Compounds Targeting the Penicillin-Binding Protein 2 (PBP2A) of Methicillin-Resistant <em>Staphylococcus aureus</em> (MRSA)Semantic proximity Read ↗

L007-0069 kills Staphylococcus aureus in high resistant phenotypes.Semantic proximity Read ↗

Structural and kinetic analysis of the monofunctional Staphylococcus aureus PBP1Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.