1ivy

From Proteopedia

Revision as of 13:35, 30 October 2007

PHYSIOLOGICAL DIMER HPP PRECURSOR

Overview

BACKGROUND: The human 'protective protein' (HPP) forms a multi-enzyme, complex with beta-galactosidase and neuraminidase in the lysosomes, protecting these two glycosidases from degradation. In humans, deficiency, of HPP leads to the lysosomal storage disease galactosialidosis., Proteolytic cleavage of the precursor form of HPP involves removal of a 2, kDa excision peptide and results in a carboxypeptidase activity. The, physiological relevance of this activity is, as yet, unknown. RESULTS: The, crystal structure of the 108 kDa dimer of the precursor HPP has been, elucidated by making extensive use of twofold density averaging. The, monomer consists of a 'core' domain and a 'cap' domain. Comparison with, the distantly related wheat serine carboxypeptidase dimer shows that the, two ... [(full description)]

About this Structure

1IVY is a [Single protein] structure of sequence from [Homo sapiens] with NAG as [ligand]. Active as [Carboxypeptidase C], with EC number [3.4.16.5]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism., Rudenko G, Bonten E, d'Azzo A, Hol WG, Structure. 1995 Nov 15;3(11):1249-59. PMID:8591035

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