1BH7
A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE
Summary for 1BH7
| Entry DOI | 10.2210/pdb1bh7/pdb |
| Descriptor | BAND 3 (1 entity in total) |
| Functional Keywords | membrane protein, cytoplasmic loop, anion exchange protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Multi-pass membrane protein: P02730 |
| Total number of polymer chains | 1 |
| Total formula weight | 4158.07 |
| Authors | Askin, D.,Bloomberg, G.B.,Chambers, E.J.,Tanner, M.J.A. (deposition date: 1998-06-16, release date: 1998-11-04, Last modification date: 2024-05-22) |
| Primary citation | Askin, D.,Bloomberg, G.B.,Chambers, E.J.,Tanner, M.J. NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3. Biochemistry, 37:11670-11678, 1998 Cited by PubMed Abstract: The membrane domain of the human red cell anion transport protein, band 3, is too large to be studied by solution nuclear magnetic resonance spectroscopy (NMR), and its amphiphilic nature requires the use of detergents for solubilization. An alternative approach is to divide the protein into smaller (trans-membrane or surface loop) domains for NMR study. We report the structure of a 46-residue synthetic peptide that corresponds to the cytoplasmic surface loop connecting the putative 12th and 13th trans-membrane spans (residues 796-841) in the 14 span model of band 3. This peptide was shown by circular dichroism (CD) to be 38% helical in 30% trifluoroacetic acid. Two regions of helix (one close to the N-terminus of the peptide and one close to the C-terminus of the peptide) were identified by NMR. Long-range nuclear Overhauser effect (NOE) cross-peaks showed the two helices to be in near proximity. The helices were separated by a proline-rich loop that exhibited local order but was mobile with respect to the rest of the peptide. We discuss how the NMR structure of this loop fits the current models of band 3 structure and topology and the results of recent mutagenesis experiments. A cyclic version of this peptide was synthesized and studied by CD, but NMR studies were not possible due to the low solubility of this peptide. PubMed: 9709005DOI: 10.1021/bi973158d PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
