2spc: Difference between revisions
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==CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN== | ==CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN== | ||
<StructureSection load='2spc' size='340' side='right' caption='[[2spc]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2spc' size='340' side='right' caption='[[2spc]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2spc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SPC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2spc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2SPC FirstGlance]. <br> | ||
</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=2spc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2spc OCA], [http://pdbe.org/2spc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2spc RCSB], [http://www.ebi.ac.uk/pdbsum/2spc PDBsum]</span></td></tr> | </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=2spc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2spc OCA], [http://pdbe.org/2spc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2spc RCSB], [http://www.ebi.ac.uk/pdbsum/2spc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2spc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sp/2spc_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sp/2spc_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> | ||
Revision as of 11:07, 12 September 2018
CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRINCRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN
Structural highlights
Function[SPTCA_DROME] 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. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane. Crystal structure of the repetitive segments of spectrin.,Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D Science. 1993 Dec 24;262(5142):2027-30. PMID:8266097[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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