Sandbox Reserved 713
From Proteopedia
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| - | ==Introduction== | + | =='''Introduction'''== |
2fkl consists in domain of the APP protein (lienentrée pdb) going from residue 126 to 189. This site play a major role in the Alzheimer disease as it is implicated in the binding of copper ion which play an important role in the production of amyloid plaques. Amyloid plaques are concentrated with Abeta peptide which results from the sequential cleavage of the APP by BACE and gamma secretase. As the interaction between copper ion and APP can modulate the production of Abeta pepetide and also the progression of Alzheimer disease, the study of the structure of the cu binding site of this protein can give a lot of informations for the developpement of novel therapeutics. | 2fkl consists in domain of the APP protein (lienentrée pdb) going from residue 126 to 189. This site play a major role in the Alzheimer disease as it is implicated in the binding of copper ion which play an important role in the production of amyloid plaques. Amyloid plaques are concentrated with Abeta peptide which results from the sequential cleavage of the APP by BACE and gamma secretase. As the interaction between copper ion and APP can modulate the production of Abeta pepetide and also the progression of Alzheimer disease, the study of the structure of the cu binding site of this protein can give a lot of informations for the developpement of novel therapeutics. | ||
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| - | ==Biological Role== | + | =='''Biological Role'''== |
| - | ==Structure== | + | =='''Structure'''== |
<Structure load='2fkl' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='2fkl' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
| Line 59: | Line 59: | ||
| - | ==Medical Implication== | + | =='''Medical Implication'''== |
| - | ==Additionnal Resources== | + | =='''Additionnal Resources'''== |
| - | ==References== | + | =='''References'''== |
| + | == '''Contributors''' == | ||
| + | Milène Walter, Andréa Mc Cann | ||
<scene name='Sandbox_Reserved_719/Tetrahedral_coordination_spher/1'>tetrahedral coordination sphere</scene> <br /> | <scene name='Sandbox_Reserved_719/Tetrahedral_coordination_spher/1'>tetrahedral coordination sphere</scene> <br /> | ||
<scene name='Sandbox_Reserved_719/Disulfide_bond/1'>disulfide bound</scene> Cys-133 and Cys-187 links strands β1 and β3 <br /> | <scene name='Sandbox_Reserved_719/Disulfide_bond/1'>disulfide bound</scene> Cys-133 and Cys-187 links strands β1 and β3 <br /> | ||
Revision as of 11:55, 3 January 2013
Alzheimer's amyloid precursor protein copper-binding domain
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| 2fkl, resolution 2.50Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Gene: | APP (Homo sapiens) | ||||||||
| Related: | 1owt, 2fjz, 2fk1, 2fk2, 2fk3 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Introduction
2fkl consists in domain of the APP protein (lienentrée pdb) going from residue 126 to 189. This site play a major role in the Alzheimer disease as it is implicated in the binding of copper ion which play an important role in the production of amyloid plaques. Amyloid plaques are concentrated with Abeta peptide which results from the sequential cleavage of the APP by BACE and gamma secretase. As the interaction between copper ion and APP can modulate the production of Abeta pepetide and also the progression of Alzheimer disease, the study of the structure of the cu binding site of this protein can give a lot of informations for the developpement of novel therapeutics.
Biological Role
Structure
|
2fkl is constituted by two chains called A and B. Both chains have the same length and the same organization. Each chain also contains an going from the residues 147 to 159 packed against a triple-strand beta sheet. The going from residues 133-139, the going from residues 162-167, and the going from residues 181 to 188. There is one more Beta sheet, B0, formed by the residues 127 to 139 of the B chain ...a compléter...
Medical Implication
Additionnal Resources
References
Contributors
Milène Walter, Andréa Mc Cann
Cys-133 and Cys-187 links strands β1 and β3
