1rh4
From Proteopedia
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| , resolution 1.9Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 13:51:33 2008
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
