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Article

Arl2-Mediated Allosteric Release of Farnesylated KRas4B from Shuttling Factor PDEδ.

The journal of physical chemistry. B - 2 Aug 2018

Ozdemir E Sila, Jang Hyunbum, Gursoy Attila, Keskin Ozlem, Nussinov Ruth

Abstract excerpt

Proper localization of Ras proteins at the plasma membrane (PM) is crucial for their functions. To get to the PM, KRas4B and some other Ras family proteins bind to the PDEδ shuttling protein through their farnesylated hypervariable regions (HVRs). The docking of their farnesyl (and to a lesser extent geranylgeranyl) in the hydrophobic pocket of PDEδ's stabilizes the interaction. At the PM, guanosine...

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Share to Allosteric Regulation
Share to Cell Membrane
Share to Cyclic Nucleotide Phosphodiesterases, Type 6

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to GTP-Binding Proteins

Share to Hydrophobic and Hydrophilic Interactions

Share to Molecular Dynamics Simulation

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Share to Proto-Oncogene Proteins p21(ras)

Source

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Identifiers

PMID: 29961325
DOI: 10.1021/acs.jpcb.8b04347
PMCID: PMC8087113

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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