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| {{STRUCTURE_1ute| PDB=1ute | SCENE= }} | | {{STRUCTURE_1ute| PDB=1ute | SCENE= }} |
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| '''PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE'''
| | ===PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE=== |
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| ==Overview==
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| BACKGROUND: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. RESULTS: The 1.55 A resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwiched beta sheets flanked by alpha-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. CONCLUSIONS: Despite less than 15% sequence identity, the protein fold resembles that of the catalytic domain of plant purple acid phosphatase and some serine/threonine protein phosphatases. The active-site regions of the mammalian and plant purple acid phosphatases differ significantly, however. The internal symmetry suggests that the binuclear centre evolved as a result of the combination of mononuclear ancestors. The structure of the mammalian enzyme provides a basis for antiosteoporotic drug design.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10425678}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10425678 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10425678}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tartrate resistant acid phosphatase]] | | [[Category: Tartrate resistant acid phosphatase]] |
| [[Category: Uteroferrin]] | | [[Category: Uteroferrin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:39:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:02:17 2008'' |
