1bb1
From Proteopedia
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| - | [[ | + | ==CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL== |
| + | <StructureSection load='1bb1' size='340' side='right' caption='[[1bb1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1bb1]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BB1 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bb1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bb1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bb1 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Electrostatic interactions are often critical for determining the specificity of protein-protein complexes. To study the role of electrostatic interactions for assembly of helical bundles, we previously designed a thermostable, heterotrimeric coiled coil, ABC, in which charged residues were employed to drive preferential association of three distinct, 34-residue helices. To investigate the basis for heterotrimer specificity, we have used multiwavelength anomalous diffraction (MAD) analysis to determine the 1.8 A resolution crystal structure of ABC. The structure shows that ABC forms a heterotrimeric coiled coil with the intended arrangement of parallel chains. Over half of the ion pairs engineered to restrict helix associations were apparent in the experimental electron density map. As seen in other trimeric coiled coils, ABC displays acute knobs-into-holes packing and a buried anion coordinated by core polar amino acids. These interactions validate the design strategy and illustrate how packing and polar contacts determine structural uniqueness. | ||
| - | + | Crystal structure of a designed, thermostable, heterotrimeric coiled coil.,Nautiyal S, Alber T Protein Sci. 1999 Jan;8(1):84-90. PMID:10210186<ref>PMID:10210186</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
[[Category: Nautiyal, S.]] | [[Category: Nautiyal, S.]] | ||
[[Category: De novo protein design]] | [[Category: De novo protein design]] | ||
Revision as of 03:25, 7 August 2014
CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL
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