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| [[Image:1bb1.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1bb1| PDB=1bb1 | SCENE= }} | | {{STRUCTURE_1bb1| PDB=1bb1 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL'''
| | ===CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10210186}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10210186 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10210186}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Coiled coil]] | | [[Category: Coiled coil]] |
| [[Category: De novo protein design]] | | [[Category: De novo protein design]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:17:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:44:35 2008'' |
