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<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | + | <StructureSection load='1xmi' size='340' side='right' caption='Caption for this structure' scene=''> | |
| - | <StructureSection load=' | + | |
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
<scene name='77/777698/Bases/1'>Nucleotide Bases</scene> | <scene name='77/777698/Bases/1'>Nucleotide Bases</scene> | ||
| + | |||
<scene name='77/777698/1xmi_scene/1'>Human F508A NBD1 domain with ATP</scene> | <scene name='77/777698/1xmi_scene/1'>Human F508A NBD1 domain with ATP</scene> | ||
| - | = | + | <scene name='77/777698/Ball_and_stick/1'>Ball and Stick</scene> |
| + | <scene name='77/777698/Mg_binding_site/1'>Magnesium</scene> | ||
| + | |||
| + | <scene name='77/777698/Phe-508/1'>Phe-508</scene> | ||
| + | |||
| + | == Function == | ||
| + | This protein is involved in chloride channel activity. It's a membrane transport protein that catalyzes the reaction: | ||
| + | ATP + H(2)O = ADP + phosphate | ||
| + | It play a large role in the function of cystic fibrosis transmembrane conductance regulator (CFTR) | ||
== Disease == | == Disease == | ||
| + | Cystic Fibrosis | ||
| + | Mutations that result in the deletion of residue Phe-508 (DeltaF508) in the first nucleotide-binding domain (NBD1) results in a severe reduction in the population of functional channels at the epithelial cell surface. The mutation is a deletion of three nucleotides spanning positions 507 and 508 of the CFTR gene on chromosome 7, which ultimately results in the loss of a single codon for the amino acid phenylalanine (F). A person with the CFTRΔF508 mutation will produce an abnormal CFTR protein that lacks this phenylalanine residue and which cannot fold properly. This protein does not escape the endoplasmic reticulum for further processing. Having two copies of this mutation (one inherited from each parent) is by far the most common cause of cystic fibrosis (CF), responsible for nearly two-thirds of cases worldwide. | ||
== Relevance == | == Relevance == | ||
Current revision
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
