Literature summary for 3.4.14.10 extracted from

Schoenegge, A.M.; Villa, E.; Foerster, F.; Hegerl, R.; Peters, J.; Baumeister, W.; Rockel, B.
The structure of human tripeptidyl peptidase II as determined by a hybrid approach (2012), Structure, 20, 593-603.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
cryoelectron microscopy and single-particle analysis show that the complex is built from two strands forming a quasihelical structure harboring a complex system of inner cavities. The dimensions of the TPP2 spindle are 55 x 28 nm and the strands are built of nine stacked dimers. The interior of each strand is permeated by a cavity system that features a suite of chambers at each dimer-dimer interface	Homo sapiens

Crystallization (Comment)

Organism

cryoelectron microscopy and single-particle analysis show that the complex is built from two strands forming a quasihelical structure harboring a complex system of inner cavities. The dimensions of the TPP2 spindle are 55 x 28 nm and the strands are built of nine stacked dimers. The interior of each strand is permeated by a cavity system that features a suite of chambers at each dimer-dimer interface

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P29144	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein with His-tag	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
erythrocyte	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
TPP2	-	Homo sapiens
tripeptidyl peptidase II	-	Homo sapiens

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Release 2023.1 (January 2023)