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1bhg

From Proteopedia

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[[Image:1bhg.gif|left|200px]]
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{{Seed}}
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[[Image:1bhg.png|left|200px]]
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{{STRUCTURE_1bhg| PDB=1bhg | SCENE= }}
{{STRUCTURE_1bhg| PDB=1bhg | SCENE= }}
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'''HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION'''
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===HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION===
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==Overview==
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The X-ray structure of the homotetrameric lysosomal acid hydrolase, human beta-glucuronidase (332,000 Mr), has been determined at 2.6 A resolution. The tetramer has approximate dihedral symmetry and each promoter consists of three structural domains with topologies similar to a jelly roll barrel, an immunoglobulin constant domain and a TIM barrel respectively. Residues 179-204 form a beta-hairpin motif similar to the putative lysosomal targeting motif of cathepsin D, supporting the view that lysosomal targeting has a structural basis. The active site of the enzyme is formed from a large cleft at the interface of two monomers. Residues Glu 451 and Glu 540 are proposed to be important for catalysis. The structure establishes a framework for understanding mutations that lead to the human genetic disease mucopolysaccharidosis VII, and for using the enzyme in anti-cancer therapy.
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The line below this paragraph, {{ABSTRACT_PUBMED_8599764}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8599764 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8599764}}
==About this Structure==
==About this Structure==
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[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Lysosomal enzyme]]
[[Category: Lysosomal enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:31:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:10:27 2008''

Revision as of 16:10, 30 June 2008

Image:1bhg.png

Template:STRUCTURE 1bhg

HUMAN BETA-GLUCURONIDASE AT 2.6 A RESOLUTION

Template:ABSTRACT PUBMED 8599764

About this Structure

1BHG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs., Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH, Nat Struct Biol. 1996 Apr;3(4):375-81. PMID:8599764

Page seeded by OCA on Mon Jun 30 19:10:27 2008

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