3edu - Revision history

OCA at 09:46, 21 February 2024

2024-02-21T09:46:59Z

← Older revision		Revision as of 09:46, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3edu' size='340' side='right'caption='[[3edu]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3edu' size='340' side='right'caption='[[3edu]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3edu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDU FirstGlance]. <br>		<table><tr><td colspan='2'>[[3edu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDU FirstGlance]. <br>
	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~SPTB~~, ~~SPTB1 (~~[~~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">X-ray diffraction, [[Resolution\|Resolution]] 2.1Å</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=3edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edu OCA], [https://pdbe.org/3edu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edu RCSB], [https://www.ebi.ac.uk/pdbsum/3edu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edu 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=3edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edu OCA], [https://pdbe.org/3edu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edu RCSB], [https://www.ebi.ac.uk/pdbsum/3edu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edu ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[https://omim.org/entry/182870 182870]]. EL3 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:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[https://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.		[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[https://omim.org/entry/182870 182870]. EL3 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:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[https://omim.org/entry/182870 182870]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_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/SPTB1_HUMAN SPTB1_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=3edu 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=3edu ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Spectrin and ankyrin participate in membrane organization, stability, signal transduction, and protein targeting; their interaction is critical for erythrocyte stability. Repeats 14 and 15 of betaI-spectrin are crucial for ankyrin recognition, yet the way spectrin binds ankyrin while preserving its repeat structure is unknown. We have solved the crystal structure of the betaI-spectrin 14,15 di-repeat unit to 2.1 A resolution and found 14 residues critical for ankyrin binding that map to the end of the helix C of repeat 14, the linker region, and the B-C loop of repeat 15. The tilt (64 degrees) across the 14,15 linker is greater than in any published di-repeat structure, suggesting that the relative positioning of the two repeats is important for ankyrin binding. We propose that a lack of structural constraints on linker and inter-helix loops allows proteins containing spectrin-like di-repeats to evolve diverse but specific ligand-recognition sites without compromising the structure of the repeat unit. The linker regions between repeats are thus critical determinants of both spectrin's flexibility and polyfunctionality. The putative coupling of flexibility and ligand binding suggests a mechanism by which spectrin might participate in mechanosensory regulation.

	The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties.,Stabach PR, Simonovic I, Ranieri MA, Aboodi MS, Steitz TA, Simonovic M, Morrow JS Blood. 2009 May 28;113(22):5377-84. Epub 2009 Jan 23. PMID:19168783<ref>PMID:19168783</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3edu" 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: Morrow~~, J S~~]]		[[Category: Morrow JS]]
	[[Category: Simonovic, I]]		[[Category: Simonovic I]]
	[[Category: Simonovic, M]]		[[Category: Simonovic M]]
	[[Category: Stabach, P]]		[[Category: Stabach P]]
	[[Category: Steitz~~, T A]]~~		[[Category: Steitz TA]]
	~~[[Category: Actin capping]]~~
	~~[[Category: Actin-binding]]~~
	~~[[Category: Ankyrin]]~~
	~~[[Category: Ankyrin-binding domain]]~~
	~~[[Category: Cytoskeleton]]~~
	~~[[Category: Disease mutation]]~~
	~~[[Category: Elliptocytosis]]~~
	~~[[Category: Hereditary hemolytic anemia]]~~
	~~[[Category: Phosphoprotein]]~~
	~~[[Category: Spectrin]]~~
	~~[[Category: Structural protein~~]]

OCA at 11:47, 16 February 2022

2022-02-16T11:47:20Z

← Older revision		Revision as of 11:47, 16 February 2022
Line 1:		Line 1:

	==Crystal structure of the ankyrin-binding domain of human erythroid spectrin==		==Crystal structure of the ankyrin-binding domain of human erythroid spectrin==
	<StructureSection load='3edu' size='340' side='right' caption='[[3edu]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3edu' size='340' side='right'caption='[[3edu]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3edu]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EDU FirstGlance]. <br>		<table><tr><td colspan='2'>[[3edu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDU FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTB, SPTB1 ([~~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">SPTB, SPTB1 ([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~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edu OCA], [~~http~~://pdbe.org/3edu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3edu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3edu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3edu 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=3edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edu OCA], [https://pdbe.org/3edu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edu RCSB], [https://www.ebi.ac.uk/pdbsum/3edu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edu ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[~~http~~://omim.org/entry/182870 182870]]. EL3 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:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[~~http~~://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.		[[https://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[https://omim.org/entry/182870 182870]]. EL3 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:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[https://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_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/SPTB1_HUMAN SPTB1_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 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Morrow, J S]]		[[Category: Morrow, J S]]
	[[Category: Simonovic, I]]		[[Category: Simonovic, I]]

OCA at 22:01, 2 December 2018

2018-12-02T22:01:54Z

← Older revision		Revision as of 22:01, 2 December 2018
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edu_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edu_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>

OCA at 08:52, 5 August 2016

2016-08-05T08:52:45Z

← Older revision		Revision as of 08:52, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of the ankyrin-binding domain of human erythroid spectrin==		==Crystal structure of the ankyrin-binding domain of human erythroid spectrin==
	<StructureSection load='3edu' size='340' side='right' caption='[[3edu]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='3edu' size='340' side='right' caption='[[3edu]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3edu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDU FirstGlance]. <br>		<table><tr><td colspan='2'>[[3edu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDU FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTB, SPTB1 ([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">SPTB, SPTB1 ([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=3edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3edu RCSB], [http://www.ebi.ac.uk/pdbsum/3edu 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=3edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edu OCA], [http://pdbe.org/3edu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3edu RCSB], [http://www.ebi.ac.uk/pdbsum/3edu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3edu ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	<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=3edu ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	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 3edu" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Morrow, J S]]		[[Category: Morrow, J S]]
	[[Category: Simonovic, I]]		[[Category: Simonovic, I]]

OCA at 14:09, 18 December 2014

2014-12-18T14:09:29Z

← Older revision		Revision as of 14:09, 18 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3edu\| PDB=3edu \| SCENE= }}~~		==Crystal structure of the ankyrin-binding domain of human erythroid spectrin==
	===Crystal structure of the ankyrin-binding domain of human erythroid spectrin===		<StructureSection load='3edu' size='340' side='right' caption='[[3edu]], [[Resolution\|resolution]] 2.10Å' scene=''>
	~~{{ABSTRACT_PUBMED_19168783}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3edu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDU FirstGlance]. <br>
	==Disease==		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SPTB, SPTB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
	[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[http://omim.org/entry/182870 182870]]. EL3 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:8226774</ref><ref>PMID:7883966</ref><ref>PMID:8018926</ref><ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[http://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.		<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=3edu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3edu RCSB], [http://www.ebi.ac.uk/pdbsum/3edu PDBsum]</span></td></tr>
			</table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[http://omim.org/entry/182870 182870]]. EL3 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:8226774</ref> <ref>PMID:7883966</ref> <ref>PMID:8018926</ref> <ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[http://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.
			== Function ==
			[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_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/ed/3edu_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 ==
			Spectrin and ankyrin participate in membrane organization, stability, signal transduction, and protein targeting; their interaction is critical for erythrocyte stability. Repeats 14 and 15 of betaI-spectrin are crucial for ankyrin recognition, yet the way spectrin binds ankyrin while preserving its repeat structure is unknown. We have solved the crystal structure of the betaI-spectrin 14,15 di-repeat unit to 2.1 A resolution and found 14 residues critical for ankyrin binding that map to the end of the helix C of repeat 14, the linker region, and the B-C loop of repeat 15. The tilt (64 degrees) across the 14,15 linker is greater than in any published di-repeat structure, suggesting that the relative positioning of the two repeats is important for ankyrin binding. We propose that a lack of structural constraints on linker and inter-helix loops allows proteins containing spectrin-like di-repeats to evolve diverse but specific ligand-recognition sites without compromising the structure of the repeat unit. The linker regions between repeats are thus critical determinants of both spectrin's flexibility and polyfunctionality. The putative coupling of flexibility and ligand binding suggests a mechanism by which spectrin might participate in mechanosensory regulation.

	~~==Function==~~		The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties.,Stabach PR, Simonovic I, Ranieri MA, Aboodi MS, Steitz TA, Simonovic M, Morrow JS Blood. 2009 May 28;113(22):5377-84. Epub 2009 Jan 23. PMID:19168783<ref>PMID:19168783</ref>
	~~[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_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==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3edu]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:/~~/~~oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA].~~		</div>

	==See Also==		==See Also==
	*[[Spectrin\|Spectrin]]		*[[Spectrin\|Spectrin]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:019168783</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Morrow, J S.]]		[[Category: Morrow, J S]]
	[[Category: Simonovic, I.]]		[[Category: Simonovic, I]]
	[[Category: Simonovic, M.]]		[[Category: Simonovic, M]]
	[[Category: Stabach, P.]]		[[Category: Stabach, P]]
	[[Category: Steitz, T A.]]		[[Category: Steitz, T A]]
	[[Category: Actin capping]]		[[Category: Actin capping]]
	[[Category: Actin-binding]]		[[Category: Actin-binding]]

OCA at 18:58, 24 March 2013

2013-03-24T18:58:18Z

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	~~[[Image:3edu.png\|left\|200px]]~~

	{{STRUCTURE_3edu\| PDB=3edu \| SCENE= }}		{{STRUCTURE_3edu\| PDB=3edu \| SCENE= }}
			===Crystal structure of the ankyrin-binding domain of human erythroid spectrin===
			{{ABSTRACT_PUBMED_19168783}}

	===~~Crystal structure~~ of the ~~ankyrin-binding domain~~ of ~~human erythroid spectrin===~~		==Disease==
			[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_HUMAN]] Defects in SPTB are the cause of elliptocytosis type 3 (EL3) [MIM:[http://omim.org/entry/182870 182870]]. EL3 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:8226774</ref><ref>PMID:7883966</ref><ref>PMID:8018926</ref><ref>PMID:1975598</ref> Defects in SPTB are the cause of spherocytosis type 2 (SPH2) [MIM:[http://omim.org/entry/182870 182870]]; also known as hereditary spherocytosis type 2 (HS2). Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH2 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.

	~~{{ABSTRACT_PUBMED_19168783}}~~		==Function==
			[[http://www.uniprot.org/uniprot/SPTB1_HUMAN SPTB1_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==
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	==Reference==		==Reference==
	<ref group="xtra">PMID:019168783</ref><references group="xtra"/>		<ref group="xtra">PMID:019168783</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Morrow, J S.]]		[[Category: Morrow, J S.]]

OCA at 19:25, 20 October 2012

2012-10-20T19:25:42Z

← Older revision		Revision as of 19:25, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[3edu]] is a 1 chain structure ~~of [[Spectrin]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA].		[[3edu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDU OCA].

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

OCA at 07:19, 27 July 2012

2012-07-27T07:19:20Z

← Older revision		Revision as of 07:19, 27 July 2012
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	[[Image:3edu.png\|left\|200px]]		[[Image:3edu.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3edu", 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_3edu\| PDB=3edu \| SCENE= }}		{{STRUCTURE_3edu\| PDB=3edu \| SCENE= }}

	===Crystal structure of the ankyrin-binding domain of human erythroid spectrin===		===Crystal structure of the ankyrin-binding domain of human erythroid spectrin===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_19168783}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 19168783 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_19168783}}		{{ABSTRACT_PUBMED_19168783}}

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	==See Also==		==See Also==
	*[[Spectrin]]		*[[Spectrin\|Spectrin]]

	==Reference==		==Reference==

OCA at 05:46, 20 July 2011

2011-07-20T05:46:17Z

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	==Reference==		==Reference==
	<ref group="xtra">PMID:~~19168783~~</ref><references group="xtra"/>		<ref group="xtra">PMID:019168783</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Morrow, J S.]]		[[Category: Morrow, J S.]]
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	[[Category: Actin capping]]		[[Category: Actin capping]]
	[[Category: Actin-binding]]		[[Category: Actin-binding]]
	~~[[Category: Alternative splicing]]~~
	[[Category: Ankyrin]]		[[Category: Ankyrin]]
	[[Category: Ankyrin-binding domain]]		[[Category: Ankyrin-binding domain]]
	~~[[Category: Cytoplasm]]~~
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]

OCA: Protected "3edu" [edit=sysop:move=sysop]

2010-12-27T00:27:56Z

Protected "3edu" [edit=sysop:move=sysop]

← Older revision	Revision as of 00:27, 27 December 2010
(No difference)