1rh4
From Proteopedia
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|PDB= 1rh4 |SIZE=350|CAPTION= <scene name='initialview01'>1rh4</scene>, resolution 1.9Å | |PDB= 1rh4 |SIZE=350|CAPTION= <scene name='initialview01'>1rh4</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=IIL:ISO-ISOLEUCINE'>IIL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh4 OCA], [http://www.ebi.ac.uk/pdbsum/1rh4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rh4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Plecs, J J.]] | [[Category: Plecs, J J.]] | ||
[[Category: Tidor, B.]] | [[Category: Tidor, B.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: IPA]] | ||
| - | [[Category: NH2]] | ||
[[Category: coiled coil]] | [[Category: coiled coil]] | ||
[[Category: de novo design]] | [[Category: de novo design]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:28:04 2008'' |
Revision as of 20:28, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 23:28:04 2008
