2A3D
SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)
Summary for 2A3D
| Entry DOI | 10.2210/pdb2a3d/pdb |
| Descriptor | PROTEIN (DE NOVO THREE-HELIX BUNDLE) (1 entity in total) |
| Functional Keywords | three-helix bundle |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 8120.13 |
| Authors | Walsh, S.T.R.,Cheng, H.,Bryson, J.W.,Roder, H.,Degrado, W.F. (deposition date: 1999-04-01, release date: 1999-05-05, Last modification date: 2023-12-27) |
| Primary citation | Walsh, S.T.,Cheng, H.,Bryson, J.W.,Roder, H.,DeGrado, W.F. Solution structure and dynamics of a de novo designed three-helix bundle protein. Proc.Natl.Acad.Sci.USA, 96:5486-5491, 1999 Cited by PubMed Abstract: 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. PubMed: 10318910DOI: 10.1073/pnas.96.10.5486 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
