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Channeling Your Inner Mutations (LB104)
Author(s) -
Brinegar Kim,
Davis Zachery,
Davidson Katie,
Fournier Ronald,
Hoover Breeanna,
Macias Nicholas,
Maldonado Vivian,
GaleaMartinez Sandra,
Grootenhuis Peter
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.lb104
Subject(s) - cystic fibrosis , cystic fibrosis transmembrane conductance regulator , mutation , chloride channel , mutant , microbiology and biotechnology , regulator , chemistry , medicine , cancer research , biology , genetics , gene , biochemistry
Approximately 70,000 people worldwide have the genetic disease cystic fibrosis (CF). CF is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR). The protein consists of two membrane spanning domains (MSD1,2), two nucleotide binding domains (NBD1,2), and a regulatory domain (R). The domains ultimately form a chloride channel. When mutant CFTR is not present at the cell surface or is dysfunctional, altered chloride levels lead to the formation of sticky mucus in the lungs, which causes chronic infection and inflammation, and ultimately death. Although there are over 1,900 CFTR mutations known, the most common is the deletion of phenylalanine‐508(F508del), which leads to the misfolding of CFTR and reduced the amount of CFTR at the cell surface. A rare mutation is the G551D mutation, which leads to defective gating of the channel. By targeting two small molecule agents, researchers have made advances in treating the underlying cause of CF. The El Capitan High School SMART (Students Modeling a Research Topic) Team used 3D printing technology to create a model of the CFTR domains based on the crystal structure of related proteins. Grant Funding Source : Supported by grants from NIH‐CTSA and NIH‐SEPA.