1bh7
From Proteopedia
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| - | [[Image:1bh7.jpg|left|200px]] | + | [[Image:1bh7.jpg|left|200px]] |
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| - | '''A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE''' | + | {{Structure |
| + | |PDB= 1bh7 |SIZE=350|CAPTION= <scene name='initialview01'>1bh7</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BH7 is a [ | + | 1BH7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH7 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9709005 9709005] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:59 2008'' |
Revision as of 08:11, 20 March 2008
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A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE
Contents |
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 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
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 Structure
1BH7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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