Sandbox Reserved 713
From Proteopedia
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| + | =Alzheimer's amyloid precursor protein copper-binding domain= | ||
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| + | ==introduction== | ||
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| + | ==Biological role== | ||
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| + | ==structure== | ||
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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 Beta 1 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 | ||
| + | ...a compléter... | ||
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| + | ==medical implication== | ||
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| + | ==additionnal resources== | ||
| + | ==References== | ||
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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' /> | ||
Revision as of 00:13, 3 January 2013
Contents |
Alzheimer's amyloid precursor protein copper-binding domain
introduction
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 alpha helix going from the residues 147 to 159 packed against a triple-strand beta sheet. The Beta 1 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 ...a compléter...
medical implication
additionnal resources
References
|
Cys-133 and Cys-187 links strands β1 and β3
