Sandbox Reserved 713
From Proteopedia
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| - | [[Image:2fkl.png|left|200px]] | + | [[Image:2fkl.png|left|200px|thumb|Caption]] |
{{STRUCTURE_2fkl| PDB=2fkl | SCENE= }} | {{STRUCTURE_2fkl| PDB=2fkl | SCENE= }} | ||
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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' /> | ||
| - | 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 | + | 2fkl is constituted by two chains called A and B<ref> PMID:12611883 </ref>. 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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| + | <ref> PMID:3290901 </ref> | ||
| - | + | <ref> PMID:12611883 </ref> | |
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=='''Medical Implication'''== | =='''Medical Implication'''== | ||
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=='''References'''== | =='''References'''== | ||
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== '''Contributors''' == | == '''Contributors''' == | ||
Revision as of 14:41, 3 January 2013
Alzheimer's amyloid precursor protein copper-binding domain
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| 2fkl, resolution 2.50Å () | |||||||||
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| 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
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2fkl is constituted by two chains called A and B[1]. 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
- ↑ Barnham KJ, McKinstry WJ, Multhaup G, Galatis D, Morton CJ, Curtain CC, Williamson NA, White AR, Hinds MG, Norton RS, Beyreuther K, Masters CL, Parker MW, Cappai R. Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. J Biol Chem. 2003 May 9;278(19):17401-7. Epub 2003 Feb 28. PMID:12611883 doi:10.1074/jbc.M300629200
- ↑ Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RA, Scolnick EM, Sigal IS. Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4686-90. PMID:3290901
- ↑ Barnham KJ, McKinstry WJ, Multhaup G, Galatis D, Morton CJ, Curtain CC, Williamson NA, White AR, Hinds MG, Norton RS, Beyreuther K, Masters CL, Parker MW, Cappai R. Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. J Biol Chem. 2003 May 9;278(19):17401-7. Epub 2003 Feb 28. PMID:12611883 doi:10.1074/jbc.M300629200
Contributors
Milène Walter, Andréa Mc Cann
Cys-133 and Cys-187 links strands β1 and β3
