1rh4
From Proteopedia
(New page: 200px<br /> <applet load="1rh4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rh4, resolution 1.9Å" /> '''RH4 DESIGNED RIGHT-H...) |
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| - | [[Image:1rh4.gif|left|200px]]<br /> | + | [[Image:1rh4.gif|left|200px]]<br /><applet load="1rh4" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rh4" size=" | + | |
caption="1rh4, resolution 1.9Å" /> | caption="1rh4, resolution 1.9Å" /> | ||
'''RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER'''<br /> | '''RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Recent advances in computational techniques have allowed the design of | + | 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== | ==About this Structure== | ||
| - | 1RH4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] with ACE, NH2 and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1RH4 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http:// | + | 1RH4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] with <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=NH2:'>NH2</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1RH4 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
| - | [[Category: Harbury, P | + | [[Category: Harbury, P B.]] |
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
| - | [[Category: Plecs, J | + | [[Category: Plecs, J J.]] |
[[Category: Tidor, B.]] | [[Category: Tidor, B.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
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[[Category: de novo design]] | [[Category: de novo design]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:50 2008'' |
Revision as of 12:50, 21 February 2008
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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 , and 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 Thu Feb 21 14:50:50 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
