Amyloid precursor protein
From Proteopedia
(Difference between revisions)
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| - | + | <StructureSection load='1mwp' size='350' side='right' scene='' caption='Human amyloid precursor protein heparin-binding domain [[1mwp]]'> | |
== Function == | == Function == | ||
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The extracellular region of APP contains several domains named E1 (residues 1-189) and E2 (residues 346-551). The E1 domain contains a growth factor-like or heparin-binding (residues 28-123) and Cu-binding (residues 124-189) subdomains. Additional domains are: Kunitz-type protease inhibitor (residues 287-344) and Zn-binding (residues 672-687). The Z-binding domain is involved in the oligomerizatin of APP. | The extracellular region of APP contains several domains named E1 (residues 1-189) and E2 (residues 346-551). The E1 domain contains a growth factor-like or heparin-binding (residues 28-123) and Cu-binding (residues 124-189) subdomains. Additional domains are: Kunitz-type protease inhibitor (residues 287-344) and Zn-binding (residues 672-687). The Z-binding domain is involved in the oligomerizatin of APP. | ||
| - | + | </StructureSection> | |
==3D structures of amyloid precursor protein== | ==3D structures of amyloid precursor protein== | ||
Revision as of 09:21, 7 December 2015
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3D structures of amyloid precursor protein
Updated on 07-December-2015
