1owa - Revision history

OCA at 08:57, 22 May 2024

OCA — Wed, 22 May 2024 08:57:32 GMT

←Older revision		Revision as of 08:57, 22 May 2024
Line 21:		Line 21:
	</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=1owa ConSurf].		</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=1owa ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We have determined the solution NMR structure of a recombinant peptide that consists of the first 156 residues of erythroid alpha-spectrin. The first 20 residues preceding the first helix (helix C') are in a disordered conformation. The subsequent three helices (helices A1, B1, and C1) form a triple helical bundle structural domain that is similar, but not identical, to previously published structures for spectrin from Drosophila and chicken brain. Paramagnetic spin label-induced NMR resonance broadening shows that helix C', the partial domain involved in alpha- and beta-spectrin association, exhibits little interaction with the structural domain. Surprisingly, helix C' is connected to helix A1 of the structural domain by a segment of 7 residues (the junction region) that exhibits a flexible disordered conformation, in contrast to the predicted rigid helical structure. We suggest that the flexibility of this particular junction region may play an important role in modulating the association affinity of alpha- and beta-spectrin at the tetramerization site of different isoforms, such as erythroid spectrin and brain spectrin. These findings may provide insight for explaining various physiological and pathological conditions that are a consequence of varying alpha- and beta-subunit self-association affinities in their formation of the various spectrin tetramers.
		+
		+	Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.,Park S, Caffrey MS, Johnson ME, Fung LW J Biol Chem. 2003 Jun 13;278(24):21837-44. Epub 2003 Apr 1. PMID:12672815<ref>PMID:12672815</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1owa" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 05:51, 17 April 2024

OCA — Wed, 17 Apr 2024 05:51:07 GMT

←Older revision		Revision as of 05:51, 17 April 2024
Line 1:		Line 1:

	==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==		==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==
-	<StructureSection load='1owa' size='340' side='right'caption='[[1owa~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='1owa' size='340' side='right'caption='[[1owa]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OWA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1owa]] 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=1OWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OWA FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>SPTA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])~~</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [https://pdbe.org/1owa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [https://www.ebi.ac.uk/pdbsum/1owa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1owa 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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [https://pdbe.org/1owa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [https://www.ebi.ac.uk/pdbsum/1owa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1owa ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[https://omim.org/entry/130600 130600]]. EL2 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:2794061</ref> <ref>PMID:8018926</ref> <ref>PMID:1679439</ref> <ref>PMID:1878597</ref> <ref>PMID:2568862</ref> <ref>PMID:1541680</ref> <ref>PMID:8364215</ref> <ref>PMID:2384601</ref> <ref>PMID:1638030</ref> <ref>PMID:2568861</ref> <ref>PMID:8193371</ref> <ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[https://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[https://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.	+	[https://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[https://omim.org/entry/130600 130600]. EL2 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:2794061</ref> <ref>PMID:8018926</ref> <ref>PMID:1679439</ref> <ref>PMID:1878597</ref> <ref>PMID:2568862</ref> <ref>PMID:1541680</ref> <ref>PMID:8364215</ref> <ref>PMID:2384601</ref> <ref>PMID:1638030</ref> <ref>PMID:2568861</ref> <ref>PMID:8193371</ref> <ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[https://omim.org/entry/266140 266140]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[https://omim.org/entry/270970 270970]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.	+	[https://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 21:
	</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=1owa ConSurf].		</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=1owa ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	We have determined the solution NMR structure of a recombinant peptide that consists of the first 156 residues of erythroid alpha-spectrin. The first 20 residues preceding the first helix (helix C') are in a disordered conformation. The subsequent three helices (helices A1, B1, and C1) form a triple helical bundle structural domain that is similar, but not identical, to previously published structures for spectrin from Drosophila and chicken brain. Paramagnetic spin label-induced NMR resonance broadening shows that helix C', the partial domain involved in alpha- and beta-spectrin association, exhibits little interaction with the structural domain. Surprisingly, helix C' is connected to helix A1 of the structural domain by a segment of 7 residues (the junction region) that exhibits a flexible disordered conformation, in contrast to the predicted rigid helical structure. We suggest that the flexibility of this particular junction region may play an important role in modulating the association affinity of alpha- and beta-spectrin at the tetramerization site of different isoforms, such as erythroid spectrin and brain spectrin. These findings may provide insight for explaining various physiological and pathological conditions that are a consequence of varying alpha- and beta-subunit self-association affinities in their formation of the various spectrin tetramers.
-
-	Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.,Park S, Caffrey MS, Johnson ME, Fung LW J Biol Chem. 2003 Jun 13;278(24):21837-44. Epub 2003 Apr 1. PMID:12672815<ref>PMID:12672815</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1owa" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Spectrin\|Spectrin]]	+	*[[Spectrin 3D structures\|Spectrin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Caffrey~~, M S~~]]	+	[[Category: Caffrey MS]]
-	[[Category: Fung~~, L W~~]]	+	[[Category: Fung LW]]
-	[[Category: Johnson~~, M E~~]]	+	[[Category: Johnson ME]]
-	[[Category: Park, S]]	+	[[Category: Park S]]
-	~~[[Category: Cytokine]]~~	+
-	~~[[Category: Triple helical bundle~~]]	+

OCA at 08:26, 23 February 2022

OCA — Wed, 23 Feb 2022 08:26:51 GMT

←Older revision		Revision as of 08:26, 23 February 2022
Line 3:		Line 3:
	<StructureSection load='1owa' size='340' side='right'caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1owa' size='340' side='right'caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1OWA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OWA FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [~~http~~://pdbe.org/1owa PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1owa PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1owa 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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [https://pdbe.org/1owa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [https://www.ebi.ac.uk/pdbsum/1owa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1owa ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[~~http~~://omim.org/entry/130600 130600]]. EL2 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:2794061</ref> <ref>PMID:8018926</ref> <ref>PMID:1679439</ref> <ref>PMID:1878597</ref> <ref>PMID:2568862</ref> <ref>PMID:1541680</ref> <ref>PMID:8364215</ref> <ref>PMID:2384601</ref> <ref>PMID:1638030</ref> <ref>PMID:2568861</ref> <ref>PMID:8193371</ref> <ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[~~http~~://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[~~http~~://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.	+	[[https://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[https://omim.org/entry/130600 130600]]. EL2 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:2794061</ref> <ref>PMID:8018926</ref> <ref>PMID:1679439</ref> <ref>PMID:1878597</ref> <ref>PMID:2568862</ref> <ref>PMID:1541680</ref> <ref>PMID:8364215</ref> <ref>PMID:2384601</ref> <ref>PMID:1638030</ref> <ref>PMID:2568861</ref> <ref>PMID:8193371</ref> <ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[https://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[https://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.	+	[[https://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:17, 9 December 2020

OCA — Wed, 09 Dec 2020 07:17:05 GMT

←Older revision		Revision as of 07:17, 9 December 2020
Line 1:		Line 1:

	==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==		==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==
-	<StructureSection load='1owa' size='340' side='right' caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>	+	<StructureSection load='1owa' size='340' side='right'caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1OWA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OWA FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://pdbe.org/1owa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1owa ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://pdbe.org/1owa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1owa ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1owa" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1owa" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Spectrin\|Spectrin]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Caffrey, M S]]		[[Category: Caffrey, M S]]
	[[Category: Fung, L W]]		[[Category: Fung, L W]]

OCA at 07:44, 15 February 2018

OCA — Thu, 15 Feb 2018 07:44:18 GMT

←Older revision		Revision as of 07:44, 15 February 2018
Line 1:		Line 1:
		+
	==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==		==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==
	<StructureSection load='1owa' size='340' side='right' caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1owa' size='340' side='right' caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OWA FirstGlance]. <br>		<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OWA FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://pdbe.org/1owa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa 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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://pdbe.org/1owa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1owa ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ow/1owa_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ow/1owa_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1owa" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1owa" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Spectrin\|Spectrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:21, 8 February 2016

OCA — Mon, 08 Feb 2016 20:21:04 GMT

←Older revision		Revision as of 20:21, 8 February 2016
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=1owa ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:03, 10 September 2015

OCA — Thu, 10 Sep 2015 15:03:42 GMT

←Older revision		Revision as of 15:03, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1owa' size='340' side='right' caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1owa' size='340' side='right' caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OWA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OWA FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa 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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://pdbe.org/1owa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		Line 28:
	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 1owa" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Caffrey, M S]]		[[Category: Caffrey, M S]]
	[[Category: Fung, L W]]		[[Category: Fung, L W]]

OCA at 07:11, 6 January 2015

OCA — Tue, 06 Jan 2015 07:11:02 GMT

←Older revision		Revision as of 07:11, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OWA FirstGlance]. <br>		<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OWA FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa 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=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[http://omim.org/entry/130600 130600]]. EL2 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:2794061</ref> <ref>PMID:8018926</ref> <ref>PMID:1679439</ref> <ref>PMID:1878597</ref> <ref>PMID:2568862</ref> <ref>PMID:1541680</ref> <ref>PMID:8364215</ref> <ref>PMID:2384601</ref> <ref>PMID:1638030</ref> <ref>PMID:2568861</ref> <ref>PMID:8193371</ref> <ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[http://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[http://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.		[[http://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[http://omim.org/entry/130600 130600]]. EL2 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:2794061</ref> <ref>PMID:8018926</ref> <ref>PMID:1679439</ref> <ref>PMID:1878597</ref> <ref>PMID:2568862</ref> <ref>PMID:1541680</ref> <ref>PMID:8364215</ref> <ref>PMID:2384601</ref> <ref>PMID:1638030</ref> <ref>PMID:2568861</ref> <ref>PMID:8193371</ref> <ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[http://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[http://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Caffrey, M S.]]	+	[[Category: Caffrey, M S]]
-	[[Category: Fung, L W.]]	+	[[Category: Fung, L W]]
-	[[Category: Johnson, M E.]]	+	[[Category: Johnson, M E]]
-	[[Category: Park, S.]]	+	[[Category: Park, S]]
	[[Category: Cytokine]]		[[Category: Cytokine]]
	[[Category: Triple helical bundle]]		[[Category: Triple helical bundle]]

OCA at 17:01, 29 September 2014

OCA — Mon, 29 Sep 2014 17:01:39 GMT

←Older revision		Revision as of 17:01, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1owa\| PDB=1owa \| SCENE= }}~~	+	==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==
-	===Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain===	+	<StructureSection load='1owa' size='340' side='right' caption='[[1owa]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_12672815}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1owa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OWA FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1owa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1owa RCSB], [http://www.ebi.ac.uk/pdbsum/1owa PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[http://omim.org/entry/130600 130600]]. EL2 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:2794061</ref> <ref>PMID:8018926</ref> <ref>PMID:1679439</ref> <ref>PMID:1878597</ref> <ref>PMID:2568862</ref> <ref>PMID:1541680</ref> <ref>PMID:8364215</ref> <ref>PMID:2384601</ref> <ref>PMID:1638030</ref> <ref>PMID:2568861</ref> <ref>PMID:8193371</ref> <ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[http://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[http://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
		+	== 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/ow/1owa_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We have determined the solution NMR structure of a recombinant peptide that consists of the first 156 residues of erythroid alpha-spectrin. The first 20 residues preceding the first helix (helix C') are in a disordered conformation. The subsequent three helices (helices A1, B1, and C1) form a triple helical bundle structural domain that is similar, but not identical, to previously published structures for spectrin from Drosophila and chicken brain. Paramagnetic spin label-induced NMR resonance broadening shows that helix C', the partial domain involved in alpha- and beta-spectrin association, exhibits little interaction with the structural domain. Surprisingly, helix C' is connected to helix A1 of the structural domain by a segment of 7 residues (the junction region) that exhibits a flexible disordered conformation, in contrast to the predicted rigid helical structure. We suggest that the flexibility of this particular junction region may play an important role in modulating the association affinity of alpha- and beta-spectrin at the tetramerization site of different isoforms, such as erythroid spectrin and brain spectrin. These findings may provide insight for explaining various physiological and pathological conditions that are a consequence of varying alpha- and beta-subunit self-association affinities in their formation of the various spectrin tetramers.

-	~~==Disease==~~	+	Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.,Park S, Caffrey MS, Johnson ME, Fung LW J Biol Chem. 2003 Jun 13;278(24):21837-44. Epub 2003 Apr 1. PMID:12672815<ref>PMID:12672815</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2~~ (~~EL2~~) ~~[MIM~~:~~[http://omim.org/entry/130600 130600]]. EL2 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:~~2794061</ref>~~<ref>PMID:~~8018926~~</ref><ref>PMID:1679439</ref><ref>PMID:1878597</ref><ref>PMID:2568862</ref><ref>PMID:1541680</ref><ref>PMID:8364215</ref><ref>PMID:2384601</ref><ref>PMID:1638030</ref><ref>PMID:2568861</ref><ref>PMID:8193371</ref><ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[http://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[http://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Spectrin is the major constituent~~ of the ~~cytoskeletal network underlying the erythrocyte plasma membrane~~. ~~It associates with band 4~~.~~1 and actin to form the cytoskeletal superstructure~~ of ~~the erythrocyte plasma membrane~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1owa]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWA OCA].~~	+

	==See Also==		==See Also==
	*[[Spectrin\|Spectrin]]		*[[Spectrin\|Spectrin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:012672815</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Caffrey, M S.]]		[[Category: Caffrey, M S.]]

OCA at 21:03, 24 March 2013

OCA — Sun, 24 Mar 2013 21:03:08 GMT

←Older revision		Revision as of 21:03, 24 March 2013
Line 1:		Line 1:
-	[[Image:1owa.png\|left\|200px]]
-
	{{STRUCTURE_1owa\| PDB=1owa \| SCENE= }}		{{STRUCTURE_1owa\| PDB=1owa \| SCENE= }}
-
	===Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain===		===Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain===
		+	{{ABSTRACT_PUBMED_12672815}}

-	~~{{ABSTRACT_PUBMED_12672815}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Defects in SPTA1 are the cause of elliptocytosis type 2 (EL2) [MIM:[http://omim.org/entry/130600 130600]]. EL2 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:2794061</ref><ref>PMID:8018926</ref><ref>PMID:1679439</ref><ref>PMID:1878597</ref><ref>PMID:2568862</ref><ref>PMID:1541680</ref><ref>PMID:8364215</ref><ref>PMID:2384601</ref><ref>PMID:1638030</ref><ref>PMID:2568861</ref><ref>PMID:8193371</ref><ref>PMID:7772539</ref> Defects in SPTA1 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:[http://omim.org/entry/266140 266140]]. HPP is an autosomal recessive disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.<ref>PMID:1878597</ref> Defects in SPTA1 are the cause of spherocytosis type 3 (SPH3) [MIM:[http://omim.org/entry/270970 270970]]; also known as hereditary spherocytosis type 3 (HS3). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SPTA1_HUMAN SPTA1_HUMAN]] Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:012672815</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012672815</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Caffrey, M S.]]		[[Category: Caffrey, M S.]]