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Diagram of a prototypical FGFR protein. Three immunoglobulin-like domains (IgI to IgIII) are indicated by loops, closed with disulfide bridges. These Iglike domains are extracellular and responsible for ligand binding. Alternative splicing in the C-terminal half of the third Ig-like loop is indicated by an extra
“half” loop. The acid box is a stretch of acidic amino acids found in all FGFRs between IgI and IgII. The tyrosine kinase domains are found intracellularly.
The tyrosine kinase A domain contains the ATP binding site. The tyrosine kinase B domain contains the catalytic site.
Source: Achondroplasia and Pseudoachondroplasia, The Online Metabolic and Molecular Bases of Inherited Disease
Citation: Valle D, Beaudet AL, Vogelstein B, Kinzler KW, Antonarakis SE, Ballabio A, Gibson K, Mitchell G. The Online Metabolic and Molecular
Bases of Inherited Disease; 2014 Available at: http://mhmedical.com/ Accessed: August 03, 2017
Copyright © 2017 McGraw-Hill Education. All rights reserved
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