Beta-amyloid precursor protein

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Presentation transcript:

Beta-amyloid precursor protein

Hydropathy plot Membrane Bound

Sequence Alignment

Sequence Alignment Beta-secretase cut site 19F and 20F AA 41 and 42

Extracellular Domain (1mwp) (1owt) Beta Sheets = green Alpha Helices = purple Links between regions color coded (1rw6)

Extracellular Domain Not much is known about the extracellular domain function. Somewhat involved with neural growth and plasticity. Found in many different cells throughout the body

Membrane Domain (1iyt) Membrane Domain is composed of two helices and turn in between Quaternary structure has overlapping alpha helices Green = amino acids 41 and 42

Membrane (Tertiary structure)

Beta-secretase (2fkn) Aspartyl protease that clips APP at the start of the membrane domain Yellow = beta sheets Pink = alpha helices Asp 32 and 215 are the active site proteases.

Side-chain interaction of Amyloid-Beta domain (1iyt) Adjacent phenylalanine residues provide hydrophobic π-stacking interactions There is also a salt bridge formed by K16 and D22 Phe 20 Phe 19

Alzheimer’s disease(2beg) Linked to buildup of amyloid-beta plaques Form complex beta-sheet fibrils

Alzheimer’s disease Tertiary structure of the Amyloid beta plaque All Beta Sheets and linkers Insoluble in cytosol and polar solvents.

References 1.) C. Morgan, M. Colombres, M. T. Nunez & N. C. Inestrosa (2004) Structure and function of amyloid in Alzheimer's disease. Progress in Neurobiology 74, 323-349. 2.) Berhanu, W. M., and Hansmann, U. H. E. (2012) Side-chain hydrophobicity and the stability of Aβ16–22 aggregates. Protein Sci. v21(12), 1837-1848. 3.) Crescenzi, O., Tomaselli, S., Guerrini, R., Salvadori, S., D'Ursi, A. M., Temussi, P. A. and Picone, D. (2002), Solution structure of the Alzheimer amyloid β-peptide (1–42) in an apolar microenvironment. European Journal of Biochemistry, 269: 5642–5648. doi: 10.1046/j.1432-1033.2002.03271.x 4.) Petkova, A. T., Yau, W., and Tycko, R., (2006) Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. NIHPA Biochemistry. 45(2), 498-512.