2spc: Difference between revisions

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 <StructureSection load='2spc' size='340' side='right'caption='[[2spc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == 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 [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. 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 [https://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2spc ProSAT]</span></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]] 1.8&#8491;</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=2spc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2spc OCA], [https://pdbe.org/2spc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2spc RCSB], [https://www.ebi.ac.uk/pdbsum/2spc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2spc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SPTCA_DROME 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.<ref>PMID:8276898</ref> <ref>PMID:3680372</ref> <ref>PMID:11076973</ref>
+[https://www.uniprot.org/uniprot/SPTCA_DROME 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.<ref>PMID:8276898</ref> <ref>PMID:3680372</ref> <ref>PMID:11076973</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=2spc ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The 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<ref>PMID:8266097</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2spc" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Spectrin|Spectrin]]
+*[[Spectrin 3D structures|Spectrin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Branton, D]]
+[[Category: Branton D]]
-[[Category: Cronin, T]]
+[[Category: Cronin T]]
-[[Category: Harrison, S C]]
+[[Category: Harrison SC]]
-[[Category: Viel, A]]
+[[Category: Viel A]]
-[[Category: Winograd, E]]
+[[Category: Winograd E]]
-[[Category: Yan, Y]]
+[[Category: Yan Y]]
-[[Category: Cytoskeleton]]