Biomaterial Database

Function, evolution and structure of multidrug resistance protein (MRP). 1997

R G Deeley, and S P Cole

Cancer Research Laboratories, Queen's University, Kingston, Ontario, Canada.

Multidrug Resistance Protein (MRP) confers resistance to natural product drugs when overexpressed in cultured cells. It has also been detected in human tumors and in some cases, expression has been correlated with a poor response to chemotherapy. MRP is present in normal tissues where it probably functions as an active transporter of amphiphilic anions. It is also presumed to transport the drugs to which it confers resistance, but how and in what form has not been resolved. Unlike other members of the ATP Binding Cassette superfamily, MRP and several related proteins have three potential membrane spanning domains. The additional NH2-proximal domain in MRP contains five membrane spanning helices with an extracytosolic NH2-terminus and is essential for transport. Conserved features of gene organization and protein structure suggest that MRP and its related proteins share their ancestry with the cystic fibrosis conductance regulator.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013329	Structure-Activity Relationship	The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.	Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D017386	Sequence Homology, Amino Acid	The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.	Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein
D018528	ATP-Binding Cassette Transporters	A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.	ABC Transporter,ABC Transporters,ATP-Binding Cassette Transporter,ATP Binding Cassette Transporter,ATP Binding Cassette Transporters,Cassette Transporter, ATP-Binding,Transporter, ABC,Transporter, ATP-Binding Cassette,Transporters, ABC,Transporters, ATP-Binding Cassette
D019143	Evolution, Molecular	The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.	Molecular Evolution,Genetic Evolution,Evolution, Genetic
D027425	Multidrug Resistance-Associated Proteins	A sequence-related subfamily of ATP-BINDING CASSETTE TRANSPORTERS that actively transport organic substrates. Although considered organic anion transporters, a subset of proteins in this family have also been shown to convey drug resistance to neutral organic drugs. Their cellular function may have clinical significance for CHEMOTHERAPY in that they transport a variety of ANTINEOPLASTIC AGENTS. Overexpression of proteins in this class by NEOPLASMS is considered a possible mechanism in the development of multidrug resistance (DRUG RESISTANCE, MULTIPLE). Although similar in function to P-GLYCOPROTEINS, the proteins in this class share little sequence homology to the ATP BINDING CASSETTE TRANSPORTER, SUBFAMILY B, MEMBER 1 family of proteins.	Multidrug Resistance-Associated Protein,ATP-Binding Cassette, Sub-Family C Proteins,MOAT Protein,Multispecific Organic Anion Transport Proteins,Multispecific Organic Anion Transporter,ATP Binding Cassette, Sub Family C Proteins,Multidrug Resistance Associated Protein,Multidrug Resistance Associated Proteins,Resistance-Associated Protein, Multidrug