Functional analysis of chimeric proteins constructed by exchanging homologous domains of two P-glycoproteins conferring distinct drug resistance profiles.

doi:10.1021/bi00141a021

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Article

Functional analysis of chimeric proteins constructed by exchanging homologous domains of two P-glycoproteins conferring distinct drug resistance profiles.

Biochemistry - 7 Jul 1992

Dhir R, Gros P

Abstract excerpt

P-Glycoproteins (P-gps) encoded by the mouse mdr1 and mdr3 (Phe939, mdr3F) genes confer distinct drug resistance profiles. While the mdr1 and mdr3F clones confer comparable levels of vinblastine (VBL) resistance, mdr3F confers actinomycin D (ACT) resistance levels 2-fold greater than mdr1, while mdr1 confers resistance to colchicine at levels 7-fold greater than mdr3F. We wished to identify in chimeric proteins...

Topics

ATP Binding Cassette Transporter, Subfamily B, Member 1
Animals
Base Sequence
Cloning, Molecular
Colchicine
Dactinomycin
Drug Resistance
Escherichia coli
Membrane Glycoproteins
Mice
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Phenotype

Protein Multimerization

Recombinant Proteins

Structure-Activity Relationship

Transfection

Transformation, Bacterial

Source

Open in PubMed

Identifiers

PMID: 1352702
DOI: 10.1021/bi00141a021

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1352702-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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