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Updated: Jun 20, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Hydrophobic interactions stabilize the basigin-MCT1 complex.

NiCole A Finch1, Paul J Linser, Judith D Ochrietor

  • 1Department of Biology, University of North Florida, 1 UNF Drive, Jacksonville, FL, 32224, USA.

The Protein Journal
|September 18, 2009
PubMed
Summary
This summary is machine-generated.

Monocarboxylate transporter-1 (MCT1) binds to Basigin's transmembrane domain. Hydrophobic residues, not glutamate, are key for this protein interaction, partially supporting prior hypotheses.

Related Experiment Videos

Last Updated: Jun 20, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Monocarboxylate transporter-1 (MCT1) is known to interact with Basigin.
  • Previous studies suggested this interaction involves Basigin's transmembrane domain, specifically a glutamate residue.

Purpose of the Study:

  • To investigate the specific amino acids in Basigin's transmembrane domain responsible for MCT1 interaction.
  • To test the hypothesis that a glutamate residue is critical for MCT1-Basigin binding.

Main Methods:

  • ELISA binding assays were performed using probes of Basigin's transmembrane domain and its fragments.
  • Site-directed mutagenesis was employed to alter candidate residues within the Basigin transmembrane domain.
  • Endogenous mouse MCT1 was used as the binding partner in the assays.

Main Results:

  • Hydrophobic residues at both the N- and C-termini of Basigin's transmembrane domain were found to interact with MCT1.
  • The specific glutamate residue previously hypothesized to be involved in the interaction was found to play no role.
  • The data confirm that Basigin's transmembrane domain is indeed involved in the interaction with MCT1.

Conclusions:

  • The transmembrane domain of Basigin is crucial for its interaction with MCT1.
  • Specific hydrophobic residues at the domain's termini mediate the MCT1-Basigin binding.
  • The hypothesis regarding the critical role of the glutamate residue was not supported by the experimental data.