1bh7: Difference between revisions
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==Overview== | ==Overview== | ||
The membrane domain of the human red cell anion transport protein, band 3, is too large to be studied by solution nuclear magnetic resonance | 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. | ||
==Disease== | ==Disease== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Askin, D.]] | [[Category: Askin, D.]] | ||
[[Category: Bloomberg, G | [[Category: Bloomberg, G B.]] | ||
[[Category: Chambers, E | [[Category: Chambers, E J.]] | ||
[[Category: Tanner, M | [[Category: Tanner, M J.A.]] | ||
[[Category: anion exchange protein]] | [[Category: anion exchange protein]] | ||
[[Category: cytoplasmic loop]] | [[Category: cytoplasmic loop]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
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Revision as of 12:55, 21 February 2008
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A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Blood group, Diego OMIM:[109270], Blood group, Froese , OMIM:[109270], Blood group, Waldner OMIM:[109270], Blood group, Wright OMIM:[109270], Diabetes insipidus, nephrogenic OMIM:[300538], Hemolytic anemia OMIM:[109270], Malaria, resistance to OMIM:[109270], Nephrogenic syndrome of inappropriate antidiuresis OMIM:[300538], Ovalocytosis OMIM:[109270], Renal tubular acidosis, distal, AD OMIM:[109270], Renal tubular acidosis, distal, AR OMIM:[109270], Spherocytosis OMIM:[109270]
About this StructureAbout this Structure
1BH7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3., Askin D, Bloomberg GB, Chambers EJ, Tanner MJ, Biochemistry. 1998 Aug 18;37(33):11670-8. PMID:9709005
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