1ba4 Summary

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THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1-40) IN A WATER-MICELLE ENVIRONMENT. IS THE MEMBRANE-SPANNING DOMAIN WHERE WE THINK IT IS? NMR, 10 STRUCTURES

The structure was published by Coles, M., Bicknell, W., Watson, A.A., Fairlie, D.P., and Craik, D.J., in 1998 in a paper entitled "Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?" (abstract).

The structure was determined using NMR spectroscopy and deposited in 1998.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of AMYLOID BETA-PEPTIDE. This molecule has the UniProt identifier P05067 (A4_HUMAN)search. The sample contained 40 residues which is < 90% of the natural sequence. Out of 40 residues 40 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A AMYLOID BETA-PEPTIDE P05067 (672-711) (A4_HUMAN)search Homo sapienssearch < 90% 40 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05067 (672 - 711) AMYLOID BETA-PEPTIDE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Amyloid peptidessearch Amyloid A4search Beta-amyloid peptide (beta-APP)search

Chain ID Cellular component (GO)
A (P05067) integral to membranesearch

Chain InterPro annotation
A Amyloidogenic glycoprotein, amyloid-beta peptidesearch