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== | ==A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE== | ||
<StructureSection load='1bh7' size='340' side='right'caption='[[1bh7]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1bh7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BH7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh7 OCA], [https://pdbe.org/1bh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bh7 RCSB], [https://www.ebi.ac.uk/pdbsum/1bh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bh7 ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN] Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:[https://omim.org/entry/109270 109270]. EL4 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.<ref>PMID:1722314</ref> <ref>PMID:1538405</ref> Defects in SLC4A1 are the cause of spherocytosis type 4 (SPH4) [MIM:[https://omim.org/entry/612653 612653]; also known as hereditary spherocytosis type 4 (HS4). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal.<ref>PMID:8547122</ref> <ref>PMID:1378323</ref> <ref>PMID:7530501</ref> <ref>PMID:8943874</ref> <ref>PMID:8640229</ref> <ref>PMID:9207478</ref> <ref>PMID:9012689</ref> <ref>PMID:9233560</ref> <ref>PMID:9973643</ref> <ref>PMID:10580570</ref> <ref>PMID:10942416</ref> <ref>PMID:10745622</ref> <ref>PMID:11380459</ref> <ref>PMID:15813913</ref> <ref>PMID:16227998</ref> Defects in SLC4A1 are the cause of renal tubular acidosis, distal, autosomal dominant (AD-dRTA) [MIM:[https://omim.org/entry/179800 179800]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. Defects in SLC4A1 are the cause of renal tubular acidosis, distal, with hemolytic anemia (dRTA-HA) [MIM:[https://omim.org/entry/611590 611590]. A disease characterized by the association of hemolytic anemia with distal renal tubular acidosis, the reduced ability to acidify urine resulting in variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. Defects in SLC4A1 are the cause of renal tubular acidosis, distal, with normal red cell morphology (dRTA-NRC) [MIM:[https://omim.org/entry/611590 611590]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN] Band 3 is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bh7_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bh7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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<ref>PMID:9709005</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1bh7" style="background-color:#fffaf0;"></div> | |||
== | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Askin | [[Category: Askin D]] | ||
[[Category: Bloomberg | [[Category: Bloomberg GB]] | ||
[[Category: Chambers | [[Category: Chambers EJ]] | ||
[[Category: Tanner | [[Category: Tanner MJA]] | ||