1rh4: Difference between revisions

Revision as of 15:50, 21 February 2008

RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1rh4, resolution 1.9&Aring;" />
 '''RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER'''<br />
 ==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.
+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==
-RH4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RH4 OCA].
+RH4 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==
@@ Line 16: / Line 15: @@
 [[Category: Synthetic construct]]
 [[Category: Alber, T.]]
-[[Category: Harbury, P.B.]]
+[[Category: Harbury, P B.]]
-[[Category: Kim, P.S.]]
+[[Category: Kim, P S.]]
-[[Category: Plecs, J.J.]]
+[[Category: Plecs, J J.]]
 [[Category: Tidor, B.]]
 [[Category: ACE]]
@@ Line 26: / Line 25: @@
 [[Category: de novo design]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:05:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:50 2008''