2a3d

SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)

spinqualitylabelsall models 2a3d, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2a3d is a 1 chain structure with sequence from Synthetic construct. The October 2005 RCSB PDB Molecule of the Month feature on Designer Proteins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_10. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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