2cw1
From Proteopedia
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| - | [[Image:2cw1.gif|left|200px]] | + | [[Image:2cw1.gif|left|200px]] |
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| - | '''Solution structure of the de novo-designed lambda Cro fold protein''' | + | {{Structure |
| + | |PDB= 2cw1 |SIZE=350|CAPTION= <scene name='initialview01'>2cw1</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of the de novo-designed lambda Cro fold protein''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CW1 is a [ | + | 2CW1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CW1 OCA]. |
==Reference== | ==Reference== | ||
| - | Design of lambda Cro fold: solution structure of a monomeric variant of the de novo protein., Isogai Y, Ito Y, Ikeya T, Shiro Y, Ota M, J Mol Biol. 2005 Dec 9;354(4):801-14. Epub 2005 Oct 21. PMID:[http:// | + | Design of lambda Cro fold: solution structure of a monomeric variant of the de novo protein., Isogai Y, Ito Y, Ikeya T, Shiro Y, Ota M, J Mol Biol. 2005 Dec 9;354(4):801-14. Epub 2005 Oct 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16289118 16289118] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ikeya, T.]] | [[Category: Ikeya, T.]] | ||
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[[Category: lambda cro fold]] | [[Category: lambda cro fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:20:24 2008'' |
Revision as of 14:20, 20 March 2008
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Solution structure of the de novo-designed lambda Cro fold protein
Overview
One of the classical DNA-binding proteins, bacteriophage lambda Cro, forms a homodimer with a unique fold of alpha-helices and beta-sheets. We have computationally designed an artificial sequence of 60 amino acid residues to stabilize the backbone tertiary structure of the lambda Cro dimer by simulated annealing using knowledge-based structure-sequence compatibility functions. The designed amino acid sequence has 25% identity with that of natural lambda Cro and preserves Phe58, which is important for formation of the stably folded structure of lambda Cro. The designed dimer protein and its monomeric variant, which was redesigned by the insertion of a beta-hairpin sequence at the C-terminal region to prevent dimerization, were synthesized and biochemically characterized to be well folded. The designed protein was monomeric under a wide range of protein concentrations and its solution structure was determined by NMR spectroscopy. The solved structure is similar to that of a monomeric variant of natural lambda Cro with a root-mean-square deviation of the polypeptide backbones at 2.1A and has a well-packed protein core. Thus, our knowledge-based functions provide approximate but essential relationships between amino acid sequences and protein structures, and are useful for finding novel sequences that are foldable into a given target structure.
About this Structure
2CW1 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Design of lambda Cro fold: solution structure of a monomeric variant of the de novo protein., Isogai Y, Ito Y, Ikeya T, Shiro Y, Ota M, J Mol Biol. 2005 Dec 9;354(4):801-14. Epub 2005 Oct 21. PMID:16289118
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