PDBsum entry 1amc

Proteinase inhibitor(trypsin)

PDB id: 1amc

Contents

Protein chain

28 a.a.

References listed in PDB file

Key reference

• Title: Solution structure of residues 1-28 of the amyloid beta-Peptide.
• Authors: J.Talafous, K.J.Marcinowski, G.Klopman, M.G.Zagorski.
• Ref.: Biochemistry, 1994, 33, 7788-7796. [DOI no: 10.1021/bi00191a006]
• PubMed id: 7516706

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.

Secondary reference #1

• Title: Nmr studies of amyloid beta-Peptides: proton assignments, Secondary structure, And mechanism of an alpha-Helix----Beta-Sheet conversion for a homologous, 28-Residue, N-Terminal fragment.
• Authors: M.G.Zagorski, C.J.Barrow.
• Ref.: Biochemistry, 1992, 31, 5621-5631. [DOI no: 10.1021/bi00139a028]
• PubMed id: 1610809

Secondary reference #2

• Title: Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition.
• Authors: C.J.Barrow, M.G.Zagorski.
• Ref.: Science, 1991, 253, 179-182. [DOI no: 10.1126/science.1853202]
• PubMed id: 1853202