Literature summary for 3.4.16.6 extracted from

Garcia-Pardo, J.; Grana-Montes, R.; Fernandez-Mendez, M.; Ruyra, A.; Roher, N.; Aviles, F.X.; Lorenzo, J.; Ventura, S.
Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions (2014), J. Biol. Chem., 289, 33783-33796.

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Cloned(Commentary)

Cloned (Comment)	Organism
the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (residues 386-460, h-TTL), is cloned into the pET-22B vector to encode a C-terminal hexahistidine fusion protein. Expression carried out in Escherichia coli	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
8700	-	gel filtration of the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL)	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Subunits

Subunits	Comment	Organism
monomer	the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) is a monomer in solution	Homo sapiens
More	the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (h-TTL) carboxypeptidase D aggregates under close to physiological conditions into amyloid structures, with the population of folded but aggregation-prone states being controlled by the conformational stability of the domain	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Carboxypeptidase D	-	Homo sapiens
CPD	-	Homo sapiens
h-TLL	the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D	Homo sapiens

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Release 2023.1 (January 2023)