View source for 1owa


==Solution Structural Studies on Human Erythrocyte Alpha Spectrin N Terminal Tetramerization Domain==
<StructureSection load='1owa' size='340' side='right'caption='[[1owa]]' scene=''>
== Structural highlights ==
<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='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>
</table>
== 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.
== 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.
== 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/main_output.php?pdb_ID=1owa ConSurf].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1owa" style="background-color:#fffaf0;"></div>

==See Also==
*[[Spectrin 3D structures|Spectrin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Caffrey MS]]
[[Category: Fung LW]]
[[Category: Johnson ME]]
[[Category: Park S]]