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

Mechanism of pKID/KIX Association Studied by Molecular Dynamics Free Energy Simulations.

The journal of physical chemistry. B - 25 Aug 2016

Bomblies Rainer, Luitz Manuel P, Zacharias Martin

Abstract excerpt

The phosphorylated kinase-inducible domain (pKID) associates with the kinase interacting domain (KIX) via a coupled folding and binding mechanism. The pKID domain is intrinsically disordered when unbound and upon phosphorylation at Ser133 binds to the KIX domain adopting a well-defined kinked two-helix structure. In order to identify putative hot spot residues of binding that could serve as an initial stable...

Read the complete abstract on PubMed

Topics

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

Share to CREB-Binding Protein
Share to Cyclic AMP Response Element-Binding Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to Protein Unfolding

Share to Thermodynamics

Source

Identifiers

PMID: 27054660
DOI: 10.1021/acs.jpcb.6b01792

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanism of pKID/KIX Association Studied by Molecular Dynamics Free Energy Simulations.PMID 27054660Read ↗

pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Semantic proximity Read ↗

Atomistic details of the disordered states of KID and pKID. Implications in coupled binding and folding.Semantic proximity Read ↗

Phosphorylation-induced transient intrinsic structure in the kinase-inducible domain of CREB facilitates its recognition by the KIX domain of CBP.Semantic proximity Read ↗

PIIMS Server: A Web Server for Mutation Hotspot Scanning at the Protein-Protein Interface.Semantic proximity Read ↗

Biophysical changes of ATP binding pocket may explain loss of kinase activity in mutant DAPK3 in cancer: A molecular dynamic simulation analysis.Semantic proximity Read ↗

Binding selectivity studies of phosphoinositide 3-kinases using free energy calculations.Semantic proximity Read ↗

A detailed thermodynamic analysis of ras/effector complex interfaces.Semantic proximity Read ↗

A model of a MAPK•substrate complex in an active conformation: a computational and experimental approach.Semantic proximity Read ↗

Hot spots in protein-protein interfaces: towards drug discovery.Semantic proximity Read ↗

Leu628 of the KIX domain of CBP is a key residue for the interaction with the MLL transactivation domain.Semantic proximity Read ↗

Structural and Dynamic Characterization of Mutated Keap1 for Varied Affinity toward Nrf2: A Molecular Dynamics Simulation Study.Semantic proximity Read ↗

Mechanism of Ser88 phosphorylation-induced dimer dissociation in dynein light chain LC8.Semantic proximity Read ↗

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