1BZK
STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN OVALOCYTOSIS.
Summary for 1BZK
| Entry DOI | 10.2210/pdb1bzk/pdb |
| Descriptor | PROTEIN (BAND 3 ANION TRANSPORT PROTEIN) (1 entity in total) |
| Functional Keywords | human erythrocyte anion transporter, transmembrane, synthetic peptide, transport protein |
| Cellular location | Membrane; Multi-pass membrane protein: P02730 |
| Total number of polymer chains | 1 |
| Total formula weight | 4628.32 |
| Authors | Chambers, E.J.,Bloomberg, G.B.,Ring, S.M.,Tanner, M.J.A. (deposition date: 1998-11-01, release date: 1999-06-01, Last modification date: 2024-11-13) |
| Primary citation | Chambers, E.J.,Bloomberg, G.B.,Ring, S.M.,Tanner, M.J. Structural studies on the effects of the deletion in the red cell anion exchanger (band 3, AE1) associated with South East Asian ovalocytosis. J.Mol.Biol., 285:1289-1307, 1999 Cited by PubMed Abstract: We have carried out a solution-state NMR study of synthetic peptides patterned on the first membrane span of normal human band 3, and the same region of the mutant band 3 present in Southeast Asian ovalocytosis (SAO) which has a nine amino acid deletion. In 1:1 (v/v) chloroform/methanol, the 42 residue normal peptide (R389-K430) consisted of three helical regions. The slow solvent exchange of backbone amide protons revealed the helix from P403 to A416 was more stable than the "cytoplasmic" N-terminal helix from P391 to A400. These helices were separated by a sharp bend at P403, which is probably located at the boundary between the cytoplasmic domain and the first transmembrane span. The SAO deletion (A400-A408) removed the bend at P403, to leave a stable helix from P391 to A416 containing the residuum of the normal first transmembrane helix and with a hydrophobic turn replaced by a polar turn in the SAO peptide. Insertion of fragments of normal band 3 and band 3 SAO into microsomal membranes was investigated using a cell free translation system. A fragment composed of the cytoplasmic domain and the putative first membrane domain of normal band 3 (B3(1)) inserted stably into the membrane. However, the corresponding fragment of band 3 SAO [SAO(1)] did not integrate stably into membranes. Our results suggest that in SAO band 3, the region of the first membrane span of normal band 3 does not integrate properly into the membrane because it lacks a sufficiently long hydrophobic segment, and the deletion also disrupts a conserved structural subdomain at the membrane surface. PubMed: 9887277DOI: 10.1006/jmbi.1998.2392 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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