Sandbox Reserved 713

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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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<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' />
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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 alpha helix going from the residues 147 to 159 packed against a triple-strand beta sheet. The <scene name='Sandbox_Reserved_719/Beta1/1'>strand beta1</scene> going from residues 133-139, the Beta 2 going from residues 162-167, and the Beta 3 going from residues 181 to 188. There is one more Beta sheet, B0, formed by the residues 127 to 139 of the B chain
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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 <scene name='Sandbox_Reserved_713/Helice_alpha/1'>alpha helix</scene> going from the residues 147 to 159 packed against a triple-strand beta sheet. The <scene name='Sandbox_Reserved_719/Beta1/1'>strand beta1</scene> going from residues 133-139, the <scene name='Sandbox_Reserved_713/Beta_stream2/1'>Beta 2</scene> going from residues 162-167, and the <scene name='Sandbox_Reserved_713/Beta_stream3/1'>Beta 3</scene> 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...
...a compléter...
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==Medical Implication==
==Medical Implication==

Revision as of 00:42, 3 January 2013

Template:Sandbox ESBS 2012

Alzheimer's amyloid precursor protein copper-binding domain


Image:2fkl.png


PDB ID 2fkl

Drag the structure with the mouse to rotate
2fkl, resolution 2.50Å ()
Gene: APP (Homo sapiens)
Related: 1owt, 2fjz, 2fk1, 2fk2, 2fk3
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

Insert caption here

Drag the structure with the mouse to rotate

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


Cys-133 and Cys-187 links strands β1 and β3

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