1btq - Revision history

OCA at 11:37, 22 November 2023

2023-11-22T11:37:25Z

←Older revision		Revision as of 11:37, 22 November 2023
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	==THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3==		==THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3==
-	<StructureSection load='1btq' size='340' side='right'caption='[[1btq~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1btq' size='340' side='right'caption='[[1btq]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1btq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1btq]] 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=1BTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTQ FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene~~></td></tr>	+	</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height~~: ~~3em;~~'>~~[[1btr\|1btr]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [https://pdbe.org/1btq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [https://www.ebi.ac.uk/pdbsum/1btq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btq 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=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [https://pdbe.org/1btq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [https://www.ebi.ac.uk/pdbsum/1btq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btq 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.	+	[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.	+	[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: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bloomberg~~, G B~~]]	+	[[Category: Bloomberg GB]]
-	[[Category: Dempsey~~, C E~~]]	+	[[Category: Dempsey CE]]
-	[[Category: Gargaro~~, A R~~]]	+	[[Category: Gargaro AR]]
-	[[Category: Murray, M]]	+	[[Category: Murray M]]
-	[[Category: Tanner~~, M J.A]]~~	+	[[Category: Tanner MJA]]
-	~~[[Category: Anion transport~~]]	+

OCA at 07:02, 24 February 2021

2021-02-24T07:02:26Z

OCA at 09:28, 21 May 2019

2019-05-21T09:28:59Z

←Older revision		Revision as of 09:28, 21 May 2019
Line 1:		Line 1:

	==THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3==		==THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3==
-	<StructureSection load='1btq' size='340' side='right' caption='[[1btq]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1btq' size='340' side='right'caption='[[1btq]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1btq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1btq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTQ FirstGlance]. <br>
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Bloomberg, G B]]		[[Category: Bloomberg, G B]]
	[[Category: Dempsey, C E]]		[[Category: Dempsey, C E]]

OCA at 06:18, 17 August 2017

2017-08-17T06:18:11Z

←Older revision		Revision as of 06:18, 17 August 2017
Line 1:		Line 1:
		+
	==THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3==		==THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3==
	<StructureSection load='1btq' size='340' side='right' caption='[[1btq]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1btq' size='340' side='right' caption='[[1btq]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1btr\|1btr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1btr\|1btr]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [http://pdbe.org/1btq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [http://www.ebi.ac.uk/pdbsum/1btq PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [http://pdbe.org/1btq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [http://www.ebi.ac.uk/pdbsum/1btq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1btq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 03:01, 10 September 2015

2015-09-10T03:01:37Z

←Older revision		Revision as of 03:01, 10 September 2015
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	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1btr\|1btr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1btr\|1btr]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [http://www.ebi.ac.uk/pdbsum/1btq PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [http://pdbe.org/1btq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [http://www.ebi.ac.uk/pdbsum/1btq PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1btq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:59, 18 December 2014

2014-12-18T12:59:29Z

←Older revision		Revision as of 12:59, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1btq\| PDB=1btq \| SCENE= }}~~	+	==THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3==
-	===THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3===	+	<StructureSection load='1btq' size='340' side='right' caption='[[1btq]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_8168533}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[1btq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BTQ FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-	[[http://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN]] Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:[http://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:[http://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:[http://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:[http://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:[http://omim.org/entry/611590 611590]]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1btr\|1btr]]</td></tr>
-		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [http://www.ebi.ac.uk/pdbsum/1btq PDBsum]</span></td></tr>
-	==Function==	+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN]] Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:[http://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:[http://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:[http://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:[http://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:[http://omim.org/entry/611590 611590]]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.
		+	== Function ==
	[[http://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.		[[http://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;">
		+	== Publication Abstract from PubMed ==
		+	We have studied the structures of synthetic peptides which correspond to the proposed first and second membrane-spanning segments of the human red cell anion transporter (band 3). The peptides, which were acetylated at their N-termini and amidated at the C-termini, comprise the 20 amino acids of residues 405-424 and 21 amino acids of residues 436-456 of the human band 3 sequence. The solution structures of the peptides in trifluoroethanol were studied by two-dimensional NMR spectroscopy. Characteristic NOEs were observed indicating that the peptides adopted a predominantly alpha-helical structure in trifluoroethanol solution. Dynamical simulated annealing using the program XPLOR was employed for the structure calculations. The amide exchange rates in trifluoroethanol have also been measured and are consistent with an alpha-helical structure for the peptides.

-	~~==About this Structure==~~	+	The solution structures of the first and second transmembrane-spanning segments of band 3.,Gargaro AR, Bloomberg GB, Dempsey CE, Murray M, Tanner MJ Eur J Biochem. 1994 Apr 1;221(1):445-54. PMID:8168533<ref>PMID:8168533</ref>
-	~~[[1btq]] is a~~ 1 ~~chain structure~~. ~~Full experimental information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:008168533</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Bloomberg, G B.]]	+	== References ==
-	[[Category: Dempsey, C E.]]	+	<references/>
-	[[Category: Gargaro, A R.]]	+	__TOC__
-	[[Category: Murray, M.]]	+	</StructureSection>
-	[[Category: Tanner, M J.A.]]	+	[[Category: Bloomberg, G B]]
		+	[[Category: Dempsey, C E]]
		+	[[Category: Gargaro, A R]]
		+	[[Category: Murray, M]]
		+	[[Category: Tanner, M J.A]]
	[[Category: Anion transport]]		[[Category: Anion transport]]

OCA at 21:34, 24 March 2013

2013-03-24T21:34:59Z

←Older revision		Revision as of 21:34, 24 March 2013
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-	[[Image:1btq.png\|left\|200px]]
-
	{{STRUCTURE_1btq\| PDB=1btq \| SCENE= }}		{{STRUCTURE_1btq\| PDB=1btq \| SCENE= }}
-
	===THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3===		===THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3===
		+	{{ABSTRACT_PUBMED_8168533}}

-	~~{{ABSTRACT_PUBMED_8168533}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN]] Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:[http://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:[http://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:[http://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:[http://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:[http://omim.org/entry/611590 611590]]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.
		+
		+	==Function==
		+	[[http://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.

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:008168533</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008168533</ref><references group="xtra"/><references/>
	[[Category: Bloomberg, G B.]]		[[Category: Bloomberg, G B.]]
	[[Category: Dempsey, C E.]]		[[Category: Dempsey, C E.]]

OCA: Protected "1btq" [edit=sysop:move=sysop]

2012-10-21T20:55:13Z

Protected "1btq" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:55, 21 October 2012

OCA at 20:55, 21 October 2012

2012-10-21T20:55:09Z

←Older revision		Revision as of 20:55, 21 October 2012
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-	{{Seed}}
	[[Image:1btq.png\|left\|200px]]		[[Image:1btq.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1btq", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1btq\| PDB=1btq \| SCENE= }}		{{STRUCTURE_1btq\| PDB=1btq \| SCENE= }}

	===THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3===		===THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_8168533}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 8168533 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_8168533}}		{{ABSTRACT_PUBMED_8168533}}

	==About this Structure==		==About this Structure==
-	~~1BTQ is a~~ [[~~Single protein~~]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA].	+	[[1btq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA].

	==Reference==		==Reference==
-	~~The solution structures of the first and second transmembrane-spanning segments of band 3., Gargaro AR, Bloomberg GB, Dempsey CE, Murray M, Tanner MJ, Eur J Biochem. 1994 Apr 1;221(1):445-54.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/8168533 8168533]~~	+	<ref group="xtra">PMID:008168533</ref><references group="xtra"/>
-	~~[[Category: Single protein]]~~	+
	[[Category: Bloomberg, G B.]]		[[Category: Bloomberg, G B.]]
	[[Category: Dempsey, C E.]]		[[Category: Dempsey, C E.]]
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	[[Category: Tanner, M J.A.]]		[[Category: Tanner, M J.A.]]
	[[Category: Anion transport]]		[[Category: Anion transport]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:42:26 2008''

OCA at 16:42, 30 June 2008

2008-06-30T16:42:28Z

←Older revision		Revision as of 16:42, 30 June 2008
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-	[[Image:1btq.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1btq.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1btq\| PDB=1btq \| SCENE= }}		{{STRUCTURE_1btq\| PDB=1btq \| SCENE= }}

-	~~'''~~THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3~~'''~~	+	===THE SOLUTION STRUCTURES OF THE FIRST AND SECOND TRANSMEMBRANE-SPANNING SEGMENTS OF BAND 3===


-	~~==Overview==~~	+	<!--
-	~~We have studied~~ the ~~structures of synthetic peptides which correspond~~ to the ~~proposed first and second membrane-spanning segments of the human red cell anion transporter~~ (~~band 3~~)~~. The peptides~~, ~~which were acetylated at their N-termini and amidated at~~ the ~~C-termini, comprise the 20 amino acids of residues 405-424 and 21 amino acids of residues 436-456 of the human band 3 sequence~~. ~~The solution structures of the peptides in trifluoroethanol were studied by two~~-~~dimensional NMR spectroscopy. Characteristic NOEs were observed indicating that the peptides adopted a predominantly alpha~~-helical structure in trifluoroethanol solution. Dynamical simulated annealing using the program XPLOR was employed for the structure calculations. The amide exchange rates in trifluoroethanol have also been measured and are consistent with an alpha-helical structure for the peptides.	+	The line below this paragraph, {{ABSTRACT_PUBMED_8168533}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 8168533 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_8168533}}

	==About this Structure==		==About this Structure==
-	1BTQ is a [[Single protein]] structure. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA].	+	1BTQ is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA].

	==Reference==		==Reference==
Line 27:		Line 31:
	[[Category: Tanner, M J.A.]]		[[Category: Tanner, M J.A.]]
	[[Category: Anion transport]]		[[Category: Anion transport]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:56:47 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:42:26 2008''

←Older revision		Revision as of 07:02, 24 February 2021
Line 3:		Line 3:
	<StructureSection load='1btq' size='340' side='right'caption='[[1btq]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1btq' size='340' side='right'caption='[[1btq]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1btq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1BTQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1btq]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTQ FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1btr\|1btr]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1btr\|1btr]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [~~http~~://pdbe.org/1btq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1btq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1btq 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=1btq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btq OCA], [https://pdbe.org/1btq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btq RCSB], [https://www.ebi.ac.uk/pdbsum/1btq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/B3AT_HUMAN B3AT_HUMAN]] Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:[~~http~~://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:[~~http~~://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:[~~http~~://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:[~~http~~://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:[~~http~~://omim.org/entry/611590 611590]]. A disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.	+	[[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 ==
-	[[~~http~~://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.	+	[[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 ==