1rh4
From Proteopedia
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RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER
Overview
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.
About this Structure
1RH4 is a Protein complex structure of sequences from Synthetic construct with ACE, NH2 and IPA as ligands. The following page contains interesting information on the relation of 1RH4 with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
High-resolution protein design with backbone freedom., Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS, Science. 1998 Nov 20;282(5393):1462-7. PMID:9822371
Page seeded by OCA on Sun Nov 18 09:05:29 2007
Categories: Designer Proteins | Protein complex | Synthetic construct | Alber, T. | Harbury, P.B. | Kim, P.S. | Plecs, J.J. | Tidor, B. | ACE | IPA | NH2 | Coiled coil | De novo design
