1s35: Difference between revisions

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[[Image:1s35.gif|left|200px]]<br /><applet load="1s35" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s35, resolution 2.40&Aring;" />
'''Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin'''<br />


==Overview==
==Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin==
Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility.
<StructureSection load='1s35' size='340' side='right'caption='[[1s35]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1s35]] 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=1S35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S35 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1s35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s35 OCA], [https://pdbe.org/1s35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s35 RCSB], [https://www.ebi.ac.uk/pdbsum/1s35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s35 ProSAT]</span></td></tr>
</table>
== 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.
== 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.
== 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/s3/1s35_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=1s35 ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Anemia, neonatal hemolytic, fatal and near-fatal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=182870 182870]], Elliptocytosis-3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=182870 182870]], Spherocytosis-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=182870 182870]]
*[[Spectrin 3D structures|Spectrin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1S35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S35 OCA].
__TOC__
 
</StructureSection>
==Reference==
Structural insights into the stability and flexibility of unusual erythroid spectrin repeats., Kusunoki H, MacDonald RI, Mondragon A, Structure. 2004 Apr;12(4):645-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15062087 15062087]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kusunoki, H.]]
[[Category: Kusunoki H]]
[[Category: MacDonald, R I.]]
[[Category: MacDonald RI]]
[[Category: Mondragon, A.]]
[[Category: Mondragon A]]
[[Category: SO4]]
[[Category: 3-helix coiled-coils]]
[[Category: alpha helical linker region]]
[[Category: beta spectrin]]
[[Category: two repeats of spectrin]]
 
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