1cun

<StructureSection load='1cun' size='340' side='right' caption='[[1cun]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1cun]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CUN FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHICKEN BRAIN MRNA FOR SPECTRIN ALPHA-CHAIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=1cun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cun OCA], [http://pdbe.org/1cun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cun RCSB], [http://www.ebi.ac.uk/pdbsum/1cun PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK]] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/1cun_consurf.spt"</scriptWhenChecked>

</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="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Spectrin is a vital component of the cytoskeleton, conferring flexibility on cells and providing a scaffold for a variety of proteins. It is composed of tandem, antiparallel coiled-coil repeats. We report four related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution of two connected repeats of chicken brain alpha-spectrin. In all of the structures, the linker region between adjacent units is alpha-helical without breaks, kinks, or obvious boundaries. Two features observed in the structures are (1) conformational rearrangement in one repeat, resulting in movement of the position of a loop, and (2) varying degrees of bending at the linker region. These features form the basis of two different models of flexibility: a conformational rearrangement and a bending model. These models provide novel atomic details of spectrin flexibility.

Structures of two repeats of spectrin suggest models of flexibility.,Grum VL, Li D, MacDonald RI, Mondragon A Cell. 1999 Aug 20;98(4):523-35. PMID:10481916<ref>PMID:10481916</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1cun" style="background-color:#fffaf0;"></div>

*[[Spectrin|Spectrin]]

[[Category: Chick]]

[[Category: Grum, V L]]

[[Category: Li, D]]

[[Category: MacDonald, R I]]

[[Category: Mondragon, A]]

[[Category: Tandem 3-helix coiled- coil]]

[[Category: Two repeats of spectrin]]