1ktb

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{{STRUCTURE_1ktb| PDB=1ktb | SCENE= }}
{{STRUCTURE_1ktb| PDB=1ktb | SCENE= }}
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'''The Structure of alpha-N-Acetylgalactosaminidase'''
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===The Structure of alpha-N-Acetylgalactosaminidase===
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==Overview==
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In the lysosome, glycosidases degrade glycolipids, glycoproteins, and oligosaccharides. Mutations in glycosidases cause disorders characterized by the deposition of undegraded carbohydrates. Schindler and Fabry diseases are caused by the incomplete degradation of carbohydrates with terminal alpha-N-acetylgalactosamine and alpha-galactose, respectively. Here we present the X-ray structure of alpha-N-acetylgalactosaminidase (alpha-NAGAL), the glycosidase that removes alpha-N-acetylgalactosamine, and the structure with bound ligand. The active site residues of alpha-NAGAL are conserved in the closely related enzyme a-galactosidase A (alpha-GAL). The structure demonstrates the catalytic mechanisms of both enzymes and reveals the structural basis of mutations causing Schindler and Fabry diseases. As alpha-NAGAL and alpha-GAL produce type O "universal donor" blood from type A and type B blood, the alpha-NAGAL structure will aid in the engineering of improved enzymes for blood conversion.
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(as it appears on PubMed at http://www.pubmed.gov), where 12005440 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12005440}}
==About this Structure==
==About this Structure==
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[[Category: Zhu, A.]]
[[Category: Zhu, A.]]
[[Category: Glycoprotein]]
[[Category: Glycoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:08:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:57:28 2008''

Revision as of 07:57, 2 July 2008

Image:1ktb.png

Template:STRUCTURE 1ktb

The Structure of alpha-N-Acetylgalactosaminidase

Template:ABSTRACT PUBMED 12005440

About this Structure

1KTB is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases., Garman SC, Hannick L, Zhu A, Garboczi DN, Structure. 2002 Mar;10(3):425-34. PMID:12005440

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