View source for 1sna


==An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein==
<StructureSection load='1sna' size='340' side='right'caption='[[1sna]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sna]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SNA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SNA 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DBZ:3-(BENZOYLAMINO)-L-ALANINE'>DBZ</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=MSO:SELENOMETHIONINE+SELENOXIDE'>MSO</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1sna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sna OCA], [https://pdbe.org/1sna PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sna RCSB], [https://www.ebi.ac.uk/pdbsum/1sna PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sna ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.

X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture.,Ali MH, Peisach E, Allen KN, Imperiali B Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12183-8. Epub 2004 Aug 9. PMID:15302930<ref>PMID:15302930</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1sna" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Ali MH]]
[[Category: Allen KN]]
[[Category: Imperiali B]]
[[Category: Peisach E]]