User:Ann Taylor/CFTR
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< User:Ann Taylor(Difference between revisions)
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==CFTR== | ==CFTR== | ||
| - | <StructureSection | + | <StructureSection scene='Model_structure' size='340' side='right' caption='Homology model of CFTR' scene=''> |
| - | The Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) is a chloride transporter that when mutated, causes cystic fibrosis. The structure of CFTR has not been determined experimentally; the structures shown on this page are based on a model built at [http://swissmodel.expasy.org]/, using the multidrug resistance protein, pgp-1 (pdb code [[4f4c]], as a model. The protein has twelve membrane spanning helices and two nucleotide binding domains. Chloride transport is regulated by both ATP and cAMP. | + | The Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) is a chloride transporter that when mutated, causes cystic fibrosis. The structure of CFTR has not been determined experimentally; the structures shown on this page are based on a model built at [http://swissmodel.expasy.org]/, using the multidrug resistance protein, pgp-1 (pdb code [[4f4c]], as a model. The protein has <scene name='72/728139/Transmembrane_section/1'>twelve membrane spanning helices</scene> and <scene name='72/728139/Nucleotide_binding_domains/1'>two nucleotide binding domains</scene>; this structure has a large <scene name='72/728139/Undefined_loop/1'>undefined loop</scene>. Chloride transport is regulated by both ATP and cAMP.<ref>PMID: 1718606</ref> |
Like most diseases, there is not a single unique mutation that leads to cystic fibrosis; rather, a wide variety of sequence alterations leads to varying disease severity.<ref>PMID: 7686820</ref> The most severe symptoms are seen in patients who do not express CFTR on the epithelial membranes, due to nonsense or frame shift mutations or splicing errors. There are also a number of mutations associated with errors in processing, including the most common mutation, F508del. Less severe symptoms are seen in patients with point mutations of <scene name='72/728139/Regulation_mutations/1'>glycines in the nucleotide binding domains</scene>; many of these changes are found in the loop regions. Changes in conduction are observed in patients with mutations of <scene name='72/728139/Arg_mutations/2'>arginines</scene> located in the membrane spanning domain that are associated with ion selectivity. | Like most diseases, there is not a single unique mutation that leads to cystic fibrosis; rather, a wide variety of sequence alterations leads to varying disease severity.<ref>PMID: 7686820</ref> The most severe symptoms are seen in patients who do not express CFTR on the epithelial membranes, due to nonsense or frame shift mutations or splicing errors. There are also a number of mutations associated with errors in processing, including the most common mutation, F508del. Less severe symptoms are seen in patients with point mutations of <scene name='72/728139/Regulation_mutations/1'>glycines in the nucleotide binding domains</scene>; many of these changes are found in the loop regions. Changes in conduction are observed in patients with mutations of <scene name='72/728139/Arg_mutations/2'>arginines</scene> located in the membrane spanning domain that are associated with ion selectivity. | ||
Current revision
CFTR
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References
- ↑ Anderson MP, Berger HA, Rich DP, Gregory RJ, Smith AE, Welsh MJ. Nucleoside triphosphates are required to open the CFTR chloride channel. Cell. 1991 Nov 15;67(4):775-84. PMID:1718606
- ↑ Welsh MJ, Smith AE. Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell. 1993 Jul 2;73(7):1251-4. PMID:7686820
