1RH4

RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER

Summary for 1RH4

• Entry DOI: 10.2210/pdb1rh4/pdb
• Descriptor: RIGHT-HANDED COILED COIL TETRAMER, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: de novo design, coiled coil
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 3817.81

Authors

Harbury, P.B.,Plecs, J.J.,Tidor, B.,Alber, T.,Kim, P.S. (deposition date: 1998-10-07, release date: 1998-12-02, Last modification date: 2024-11-20)

Primary citation

Harbury, P.B.,Plecs, J.J.,Tidor, B.,Alber, T.,Kim, P.S.
High-resolution protein design with backbone freedom.
Science, 282:1462-1467, 1998

PubMed Abstract: Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.

PubMed: 9822371
DOI: 10.1126/science.282.5393.1462

Experimental method

X-RAY DIFFRACTION (1.9 Å)