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Table 1 Location of FAD mutations within the APP-TM sequence

From: Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants

APP (709–717)

709

710

711

712

713

714

715

716

717

Wild-type sequence

G

V

v

i

A

T

v

i

V

FAD mutations in the APP-TM domain

    

T

I

m

v

F

      

A

a

t

G

         

I

         

L

  1. The segment of the APP-TM domain comprising residues 709 to 717 is shown. Residue positions that are capitalized and bolded represent positions predicted to form the dimer interface. Note that the majority of FAD mutations in the APP-TM domain occur in dimer interface positions. APP mutation references [8, 16-22].
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BMC Neuroscience

ISSN: 1471-2202

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