1xf9
From Proteopedia
(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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| - | [[Image:1xf9.gif|left|200px]]<br /><applet load="1xf9" size=" | + | [[Image:1xf9.gif|left|200px]]<br /><applet load="1xf9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xf9, resolution 2.70Å" /> | caption="1xf9, resolution 2.70Å" /> | ||
'''Structure of NBD1 from murine CFTR- F508S mutant'''<br /> | '''Structure of NBD1 from murine CFTR- F508S mutant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mutations in the cystic fibrosis transmembrane conductance regulator | + | 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== | ==About this Structure== | ||
| - | 1XF9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG, ATP and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XF9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XF9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brautigam, C | + | [[Category: Brautigam, C A.]] |
[[Category: Machius, M.]] | [[Category: Machius, M.]] | ||
| - | [[Category: Thibodeau, P | + | [[Category: Thibodeau, P H.]] |
| - | [[Category: Thomas, P | + | [[Category: Thomas, P J.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
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[[Category: nucleotide-binding domain]] | [[Category: nucleotide-binding domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:08 2008'' |
Revision as of 13:54, 21 February 2008
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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 , and 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
Page seeded by OCA on Thu Feb 21 15:54:08 2008
