2btb
From Proteopedia
(Difference between revisions)
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==NMR STUDY OF N-TERMINAL HUMAN BAND 3 PEPTIDE, RESIDUES 1-15== | ==NMR STUDY OF N-TERMINAL HUMAN BAND 3 PEPTIDE, RESIDUES 1-15== | ||
- | <StructureSection load='2btb' size='340' side='right'caption='[[2btb | + | <StructureSection load='2btb' size='340' side='right'caption='[[2btb]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2btb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2btb]] 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=2BTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BTB FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </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=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=2btb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btb OCA], [https://pdbe.org/2btb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2btb RCSB], [https://www.ebi.ac.uk/pdbsum/2btb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2btb ProSAT]</span></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=2btb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btb OCA], [https://pdbe.org/2btb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2btb RCSB], [https://www.ebi.ac.uk/pdbsum/2btb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2btb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == 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 == | == 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. | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Post | + | [[Category: Post CB]] |
- | [[Category: Schneider | + | [[Category: Schneider ML]] |
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Revision as of 16:33, 13 December 2023
NMR STUDY OF N-TERMINAL HUMAN BAND 3 PEPTIDE, RESIDUES 1-15
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