Literature summary for 3.4.11.21 extracted from

Chaikuad, A.; Pilka, E.; De Riso, A.; Von Delft, F.; Kavanagh, K.; Venien-Bryan, C.; Oppermann, U.; Yue, W.
Structure of human aspartyl aminopeptidase complexed with substrate analogue: Insight into catalytic mechanism, substrate specificity and M18 peptidase family (2012), BMC Struct. Biol., 12, 14.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with zinc and substrate analogue aspartate-beta-hydroxamate, to 2.2 A resolution. Structure reveals a dodecameric machinery built by domain-swapped dimers, in agreement with electron microscopy data. For both Asp-Ala and Glu-Ala substrates, the Asp and Glu side chains fit into the P1 substrate pocket without steric constraints, while the main chain is modeled onto the hydroxamate group of aspartate-beta-hydroxamate in a position optimal for hydrolysis. The P1 substrate pocket is created by strand beta15 and the beta16-alpha12 and beta17-alpha13 loops, with the beta17-lpha13 loop lining the wall and restricting the dimensions of the pocket. This limited space disfavours bulky hydrophobic residues	Homo sapiens

Crystallization (Comment)

Organism

in complex with zinc and substrate analogue aspartate-beta-hydroxamate, to 2.2 A resolution. Structure reveals a dodecameric machinery built by domain-swapped dimers, in agreement with electron microscopy data. For both Asp-Ala and Glu-Ala substrates, the Asp and Glu side chains fit into the P1 substrate pocket without steric constraints, while the main chain is modeled onto the hydroxamate group of aspartate-beta-hydroxamate in a position optimal for hydrolysis. The P1 substrate pocket is created by strand beta15 and the beta16-alpha12 and beta17-alpha13 loops, with the beta17-lpha13 loop lining the wall and restricting the dimensions of the pocket. This limited space disfavours bulky hydrophobic residues

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9ULA0	-	-

Synonyms

Synonyms	Comment	Organism
DNPEP	-	Homo sapiens

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Release 2023.1 (January 2023)