A structural study of the carboxyl terminal region of the human erythrocyte band 3 protein. 1995

A Mori, and K Okubo, and D Kang, and N Hamasaki
Department of Clinical Chemistry, Kyushu University, Fukuoka.

Two peptides derived from the carboxyl terminal region of the human erythrocyte band 3 protein were identified as fragments releasable from cell membranes on trypsin digestion. These peptides, Asn-880-Lys-892 and Ala-893-Val-911-COOH, however, were resistant to trypsin, unless the cell membranes had been treated with high concentrations of NaOH. This suggests that the carboxyl terminal region is located in situ within the native band 3 molecule. Unlike in the cases of other portions of the band 3 protein, such as Gly-647-Arg-656, Ser-731-Lys-743, and Tyr-818-Lys-826, the release of the carboxyl terminal region was not inhibited by pretreatment of erythrocytes with 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS), indicating that there is no major structural difference in the carboxyl terminal portion between the outward and inward facing forms. The carboxyl terminal region of the band 3 protein has a negative charge cluster. In the middle of the negative charge cluster, consensus sequences, Val-Asp-X-X-X-Leu-Asp-Ala-Asp-Asp and Thr-Phe-Asp-Glu (TFDE), were found in the carboxyl terminal regions of aquaporin CHIP and glucose transporter 1, respectively. The sequence, TFDE, exists in the highly amphipathic 11-residue sequence of glucose transporter 1, and this amphipathic sequence has been suggested to promote normal membrane insertion of polytopic membrane proteins such as glucose transporter 1 and serine chemoreceptor. The role of the carboxyl terminal region of the band 3 protein is discussed.

UI MeSH Term Description Entries
D008239 Lysine An essential amino acid. It is often added to animal feed. Enisyl,L-Lysine,Lysine Acetate,Lysine Hydrochloride,Acetate, Lysine,L Lysine
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
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010449 Peptide Mapping Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases. Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
D003488 Cyanogen Bromide Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes. Bromide, Cyanogen
D004910 Erythrocyte Membrane The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS. Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000409 Alanine A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM. Abufène,Alanine, L-Isomer,L-Alanine,Alanine, L Isomer,L Alanine,L-Isomer Alanine
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

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