1AMB

SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE

Summary for 1AMB

• Entry DOI: 10.2210/pdb1amb/pdb
• Descriptor: AMYLOID BETA-PEPTIDE (1 entity in total)
• Functional Keywords: proteinase inhibitor(trypsin)
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P05067
• Total number of polymer chains: 1
• Total formula weight: 3268.51

Authors

Talafous, J.,Marcinowski, K.J.,Klopman, G.,Zagorski, M.G. (deposition date: 1994-10-21, release date: 1994-12-20, Last modification date: 2024-05-22)

Primary citation

Talafous, J.,Marcinowski, K.J.,Klopman, G.,Zagorski, M.G.
Solution structure of residues 1-28 of the amyloid beta-peptide.
Biochemistry, 33:7788-7796, 1994

PubMed Abstract: The three-dimensional solution structure of residues 1-28 of the amyloid beta-peptide was determined using nuclear magnetic resonance spectroscopy, distance geometry, and molecular dynamic techniques. The nuclear magnetic resonance data used to derive the structure consisted of nuclear Overhauser enhancements, vicinal coupling constants, and temperature coefficients of the amide-NH chemical shifts. The beta-peptide is the major proteinaceous component of amyloid deposits in Alzheimer's disease. In membrane-like media, the peptide folds to form a predominately alpha-helical structure with a bend centered at residue 12. The side chains of histidine-13 and lysine-16 are close, residing on the same face of the helix. Their proximity may constitute a binding motif with the heparan sulfate proteoglycans. The molecular details of the structure shown here could facilitate the design of rational treatments to curtail the binding of heparan sulfate proteoglycans or to prevent an alpha-helix-->beta-sheet conversion that may occur during the early stages of amyloid formation in Alzheimer's disease.

PubMed: 7516706
DOI: 10.1021/bi00191a006

Experimental method

SOLUTION NMR