1xf9
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(New page: 200px<br /><applet load="1xf9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xf9, resolution 2.70Å" /> '''Structure of NBD1 fr...)
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Revision as of 03:55, 21 November 2007
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Structure of NBD1 from murine CFTR- F508S mutant
Overview
Mutations in the cystic fibrosis transmembrane conductance regulator, (CFTR), an integral membrane protein, cause cystic fibrosis (CF). The most, common CF-causing mutant, deletion of Phe508, fails to properly fold. To, elucidate the role Phe508 plays in the folding of CFTR, missense mutations, at this position were generated. Only one missense mutation had a, pronounced effect on the stability and folding of the isolated domain in, vitro. In contrast, many substitutions, including those of charged and, bulky residues, disrupted folding of full-length CFTR in cells. Structures, of two mutant nucleotide-binding domains (NBDs) reveal only local, alterations of the surface near position 508. These results suggest that, the peptide backbone plays a role in the proper folding of the domain, whereas the side chain plays a role in defining a surface of NBD1 that, potentially interacts with other domains during the maturation of intact, CFTR.
About this Structure
1XF9 is a Single protein structure of sequence from Mus musculus with MG, ATP and ACY as ligands. Full crystallographic information is available from OCA.
Reference
Side chain and backbone contributions of Phe508 to CFTR folding., Thibodeau PH, Brautigam CA, Machius M, Thomas PJ, Nat Struct Mol Biol. 2005 Jan;12(1):10-6. Epub 2004 Dec 26. PMID:15619636
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