1LYY

AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME

Summary for 1LYY

Entry DOI	10.2210/pdb1lyy/pdb
Descriptor	LYSOZYME (2 entities in total)
Functional Keywords	hydrolase, enzyme, beta-1, 4-glycan-hydrolase
Biological source	Homo sapiens (human)
Cellular location	Secreted: P61626
Total number of polymer chains	1
Total formula weight	14743.75
Authors	Sunde, M.,Blake, C.C.F. (deposition date: 1997-01-16, release date: 1997-04-01, Last modification date: 2024-11-20)
Primary citation	Booth, D.R.,Sunde, M.,Bellotti, V.,Robinson, C.V.,Hutchinson, W.L.,Fraser, P.E.,Hawkins, P.N.,Dobson, C.M.,Radford, S.E.,Blake, C.C.,Pepys, M.B. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature, 385:787-793, 1997 Cited by PubMed Abstract: Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally. PubMed: 9039909 DOI: 10.1038/385787a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation