2jm0
From Proteopedia
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|PDB= 2jm0 |SIZE=350|CAPTION= <scene name='initialview01'>2jm0</scene> | |PDB= 2jm0 |SIZE=350|CAPTION= <scene name='initialview01'>2jm0</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=PF5:2,3,4,5,6-PENTAFLUORO-L-PHENYLALANINE'>PF5</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jm0 OCA], [http://www.ebi.ac.uk/pdbsum/2jm0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jm0 RCSB]</span> | ||
}} | }} | ||
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[[Category: vhp]] | [[Category: vhp]] | ||
| - | ''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 03:59:00 2008'' |
Revision as of 00:59, 31 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of chicken villin headpiece subdomain containing a fluorinated side chain in the core
Overview
We report the first high-resolution structure for a protein containing a fluorinated side chain. Recently we carried out a systematic evaluation of phenylalanine to pentafluorophenylalanine (Phe --> F(5)-Phe) mutants for the 35-residue chicken villin headpiece subdomain (c-VHP), the hydrophobic core of which features a cluster of three Phe side chains (residues 6, 10, and 17). Phe --> F(5)-Phe mutations are interesting because aryl-perfluoroaryl interactions of optimal geometry are intrinsically more favorable than either aryl-aryl or perfluoroaryl-perfluoroaryl interactions, and because perfluoroaryl units are more hydrophobic than are analogous aryl units. Only one mutation, Phe10 --> F(5)-Phe, was found to provide enhanced tertiary structural stability relative to the native core (by approximately 1 kcal/mol, according to guanidinium chloride denaturation studies). The NMR structure of this mutant, described here, reveals very little variation in backbone conformation or side chain packing relative to the wild type. Thus, although Phe --> F(5)-Phe mutations offer the possibility of greater tertiary structural stability from side chain-side chain attraction and/or side chain desolvation, the constraints associated with the native c-VHP fold apparently prevent the modified polypeptide from taking advantage of this possibility. Our findings are important because they complement several studies that have shown that fluorination of saturated side chain carbon atoms can provide enhanced conformational stability.
About this Structure
2JM0 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of a small protein containing a fluorinated side chain in the core., Cornilescu G, Hadley EB, Woll MG, Markley JL, Gellman SH, Cornilescu CC, Protein Sci. 2007 Jan;16(1):14-9. Epub 2006 Nov 22. PMID:17123960
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