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Article

The association of polar residues in the DAP12 homodimer: TOXCAT and molecular dynamics simulation studies.

Biophysical journal - 2 Apr 2013

Wei Peng, Zheng Bo-Kai, Guo Peng-Ru, Kawakami Toru, Luo Shi-Zhong

Abstract excerpt

Dimerization of the transmembrane (TM) adaptor protein DAP12 plays a key role in mediating activation signals through TM-TM association with cell-surface receptors. Herein, we apply the TOXCAT assay and molecular dynamics simulation to analyze dynamics and dimerization of the TM helix of DAP12 in the membrane bilayer. In the TOXCAT assay, we performed site-specific mutagenesis of potential dimerization motifs in...

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Share to Adaptor Proteins, Signal Transducing
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipid Bilayers

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Share to Mutagenesis, Site-Directed

Share to Protein Multimerization

Share to Protein Structure, Quaternary

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Source

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Identifiers

PMID: 23561520
DOI: 10.1016/j.bpj.2013.01.054
PMCID: PMC3617422

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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