Cystic fibrosis transmembrane conductance regulator (CFTR)

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CFTR is a mostly <scene name='78/785332/Secondary_structure/1'>alpha helical</scene> protein. The membrane spanning segments can be clearly seen with coloring by <scene name='78/785332/Hydrophobicity/1'>hydrophobicity</scene>, which shows hydrophobic residues in gray and hydrophilic residues in purple.
CFTR is a mostly <scene name='78/785332/Secondary_structure/1'>alpha helical</scene> protein. The membrane spanning segments can be clearly seen with coloring by <scene name='78/785332/Hydrophobicity/1'>hydrophobicity</scene>, which shows hydrophobic residues in gray and hydrophilic residues in purple.
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One feature of the CFTR is a Walker motif, which is found in ATP binding proteins.It is also known as a P (or phosphate binding) loop.
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The extracellular end of the channel has several <scene name='78/785332/Ec_cl_selection/1'>positively charged</scene> residues that are important for recruiting chloride ions to the channel. A number of <scene name='78/785332/Plus_channel/1'>positively charged</scene> residues line the channel. One feature of the CFTR is a Walker motif, which is found in ATP binding proteins.It is also known as a P (or phosphate binding) loop.
==3D Printed Physical Model of the CFTR protein==
==3D Printed Physical Model of the CFTR protein==

Revision as of 21:05, 16 October 2019

Cystic fibrosis transmembrane conductance regulator (CFTR)

Cystic Fibrosis Transmembrane Conductance regulator

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References

Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Mark Hoelzer, Michal Harel

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