1xf9
From Proteopedia
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| - | [[Image:1xf9.gif|left|200px]] | + | [[Image:1xf9.gif|left|200px]] |
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| - | '''Structure of NBD1 from murine CFTR- F508S mutant''' | + | {{Structure |
| + | |PDB= 1xf9 |SIZE=350|CAPTION= <scene name='initialview01'>1xf9</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= Cftr, Abcc7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of NBD1 from murine CFTR- F508S mutant''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XF9 is a [ | + | 1XF9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XF9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15619636 15619636] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
| - | [[Category: abc | + | [[Category: abc transporter]] |
[[Category: atp]] | [[Category: atp]] | ||
[[Category: cystic fibrosis]] | [[Category: cystic fibrosis]] | ||
[[Category: nucleotide-binding domain]] | [[Category: nucleotide-binding domain]] | ||
| - | ''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 15:09:04 2008'' |
Revision as of 13:09, 20 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | Cftr, Abcc7 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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