1tkn Summary


Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein

The structure was published by Dulubova, I., Ho, A., Huryeva, I., Sudhof, T.C., and Rizo, J., in 2004 in a paper entitled "Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2004.

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

The PDB entry contains the structure of Amyloid beta A4 protein. This molecule has the UniProt identifier P05067 (A4_HUMAN)search. The sample contained 110 residues which is < 90% of the natural sequence. Out of 110 residues 110 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 A4 protein P05067 (460-569) (A4_HUMAN)search Homo sapienssearch < 90% 110 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05067 (460 - 569) Amyloid beta A4 protein Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A CAPPD, an extracellular domain of amyloid beta A4 proteinsearch E2 domain of amyloid precursor proteinsearch

Chain ID Biological process (GO)
A (P05067) nervous system developmentsearch

Chain InterPro annotation
A Amyloidogenic glycoprotein, E2 domainsearch Amyloid beta A4 proteinsearch