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==Overview==

Amyloid beta-peptide, which forms neuronal and vascular amyloid deposits, in Alzheimer's disease, is derived from an integral membrane protein, precursor. The biological function of the precursor is currently unclear., Here we describe the X-ray structure of E2, the largest of the three, conserved domains of the precursor. The structure of E2 consists of two, coiled-coil substructures connected through a continuous helix and bears, an unexpected resemblance to the spectrin family of protein structures. E2, can reversibly dimerize in the solution, and the dimerization occurs along, the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against, the C-terminal substructure of a second monomer. Heparan sulfate, proteoglycans, the putative ligand for the precursor present in, extracellular matrix, bind to E2 at a conserved and positively charged, site near the dimer interface.

Amyloid beta-peptide, which forms neuronal and vascular amyloid deposits in Alzheimer's disease, is derived from an integral membrane protein precursor. The biological function of the precursor is currently unclear. Here we describe the X-ray structure of E2, the largest of the three conserved domains of the precursor. The structure of E2 consists of two coiled-coil substructures connected through a continuous helix and bears an unexpected resemblance to the spectrin family of protein structures. E2 can reversibly dimerize in the solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. Heparan sulfate proteoglycans, the putative ligand for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.

==About this Structure==

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[[Category: dimer]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Amyloid beta-peptide, which forms neuronal and vascular amyloid deposits, in Alzheimer's disease, is derived from an integral membrane protein, precursor. The biological function of the precursor is currently unclear., Here we describe the X-ray structure of E2, the largest of the three, conserved domains of the precursor. The structure of E2 consists of two, coiled-coil substructures connected through a continuous helix and bears, an unexpected resemblance to the spectrin family of protein structures. E2, can reversibly dimerize in the solution, and the dimerization occurs along, the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against, the C-terminal substructure of a second monomer. Heparan sulfate, proteoglycans, the putative ligand for the precursor present in, extracellular matrix, bind to E2 at a conserved and positively charged, site near the dimer interface.
+Amyloid beta-peptide, which forms neuronal and vascular amyloid deposits in Alzheimer's disease, is derived from an integral membrane protein precursor. The biological function of the precursor is currently unclear. Here we describe the X-ray structure of E2, the largest of the three conserved domains of the precursor. The structure of E2 consists of two coiled-coil substructures connected through a continuous helix and bears an unexpected resemblance to the spectrin family of protein structures. E2 can reversibly dimerize in the solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. Heparan sulfate proteoglycans, the putative ligand for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.
 ==About this Structure==
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 [[Category: dimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:50:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:11 2008''