3l1e

<StructureSection load='3l1e' size='340' side='right' caption='[[3l1e]], [[Resolution|resolution]] 1.15&Aring;' scene=''>

<table><tr><td colspan='2'>[[3l1e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. The July 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Crystallins'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_7 10.2210/rcsb_pdb/mom_2010_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L1E FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l1f|3l1f]], [[3l1g|3l1g]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRYA1, CRYAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=3l1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l1e OCA], [http://pdbe.org/3l1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l1e RCSB], [http://www.ebi.ac.uk/pdbsum/3l1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l1e ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CRYAA_BOVIN CRYAA_BOVIN]] May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

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== Publication Abstract from PubMed ==

Small heat shock proteins alphaA and alphaB crystallin form highly polydisperse oligomers that frustrate protein aggregation, crystallization, and amyloid formation. Here, we present the crystal structures of truncated forms of bovine alphaA crystallin (AAC(59-163)) and human alphaB crystallin (ABC(68-162)), both containing the C-terminal extension that functions in chaperone action and oligomeric assembly. In both structures, the C-terminal extensions swap into neighboring molecules, creating runaway domain swaps. This interface, termed DS, enables crystallin polydispersity because the C-terminal extension is palindromic and thereby allows the formation of equivalent residue interactions in both directions. That is, we observe that the extension binds in opposite directions at the DS interfaces of AAC(59-163) and ABC(68-162). A second dimeric interface, termed AP, also enables polydispersity by forming an antiparallel beta sheet with three distinct registration shifts. These two polymorphic interfaces enforce polydispersity of alpha crystallin. This evolved polydispersity suggests molecular mechanisms for chaperone action and for prevention of crystallization, both necessary for transparency of eye lenses.

 

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== References ==

[[Category: Bovin]]

[[Category: Cascio, D]]

[[Category: Eisenberg, D]]

[[Category: Laganowsky, A]]

[[Category: Sawaya, M R]]

[[Category: Protein aggregation]]