2a3d | pdb_00002a3d
SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)
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Overview
Although de novo protein design is an important endeavor with implications, for understanding protein folding, until now, structures have been, determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle, protein, alpha3D, is reported. The structure of alpha3D was not based on, any natural protein, and yet it shows thermodynamic and spectroscopic, properties typical of native proteins. A variety of features contribute to, its unique structure, including electrostatics, the packing of a diverse, set of hydrophobic side chains, and a loop that incorporates common, capping motifs. Thus, it is now possible to design a complex protein with, a well defined and predictable three-dimensional structure.
About this Structure
2A3D is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 2A3D with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
Solution structure and dynamics of a de novo designed three-helix bundle protein., Walsh ST, Cheng H, Bryson JW, Roder H, DeGrado WF, Proc Natl Acad Sci U S A. 1999 May 11;96(10):5486-91. PMID:10318910
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