J Mol Biol. 1992 Sep 5;227(1):265-70.

Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme.

Gulnik S, Baldwin ET, Tarasova N, Erickson J.

Source

Structural Biochemistry Program, PRI/DynCorp, NCI-FCRDC, Frederick, MD 21702.

Abstract

The two-chain form of active cathepsin D, a glycosylated, lysosomal aspartic proteinase, has been isolated from human liver. Isoelectric focusing revealed two major species of enzyme that differed by approximately 0.2 pI unit. Crystals suitable for X-ray diffraction analysis were prepared from acidic solutions using precipitation with ammonium sulfate. The hexagonal crystals diffracted X-rays to beyond 3.1 A resolution and belonged to space group P6(1) (or P6(5)) with cell constants a = b = 125.9 A, c = 104.1 A, gamma = 120.0 degrees. The crystals likely contain two molecules in the asymmetric unit, giving a solvent content of 56% (v/w). Biochemical analysis of crystals indicated that both isoforms were present in approximately equimolar proportions. Full structure determination of the enzyme is underway.

PMID:: 1522590; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

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Research Support, U.S. Gov't, P.H.S.

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Cathepsin D

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Cited by 3 PubMed Central articles

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Structures reported by this article

Cathepsin D At Ph 7.5

PDB: 1LYW

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 2.5 Å

See all 3 structures...

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J Mol Biol. 1992 Sep 5 ;227(1):265-70.

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