1vjq
From Proteopedia
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|GENE= | |GENE= | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02244 Propep_M14]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02244 Propep_M14]</span> | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vjq OCA], [http://www.ebi.ac.uk/pdbsum/1vjq PDBsum | + | |RELATEDENTRY= |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vjq OCA], [http://www.ebi.ac.uk/pdbsum/1vjq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vjq RCSB]</span> | ||
}} | }} | ||
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[[Category: structural genomics of pathogenic protozoa consortium]] | [[Category: structural genomics of pathogenic protozoa consortium]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:25:24 2008'' |
Revision as of 21:25, 30 March 2008
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| , resolution 2.098Å | |||||||
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| Ligands: | |||||||
| Domains: | Propep_M14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Designed protein based on backbone conformation of procarboxypeptidase-A (1AYE) with sidechains chosen for maximal predicted stability.
Overview
A previously developed computer program for protein design, RosettaDesign, was used to predict low free energy sequences for nine naturally occurring protein backbones. RosettaDesign had no knowledge of the naturally occurring sequences and on average 65% of the residues in the designed sequences differ from wild-type. Synthetic genes for ten completely redesigned proteins were generated, and the proteins were expressed, purified, and then characterized using circular dichroism, chemical and temperature denaturation and NMR experiments. Although high-resolution structures have not yet been determined, eight of these proteins appear to be folded and their circular dichroism spectra are similar to those of their wild-type counterparts. Six of the proteins have stabilities equal to or up to 7kcal/mol greater than their wild-type counterparts, and four of the proteins have NMR spectra consistent with a well-packed, rigid structure. These encouraging results indicate that the computational protein design methods can, with significant reliability, identify amino acid sequences compatible with a target protein backbone.
About this Structure
1VJQ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins., Dantas G, Kuhlman B, Callender D, Wong M, Baker D, J Mol Biol. 2003 Sep 12;332(2):449-60. PMID:12948494 [[Category: ]]
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