1lyw
From Proteopedia
(New page: 200px<br /> <applet load="1lyw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lyw, resolution 2.5Å" /> '''CATHEPSIN D AT PH 7....) |
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caption="1lyw, resolution 2.5Å" /> | caption="1lyw, resolution 2.5Å" /> | ||
'''CATHEPSIN D AT PH 7.5'''<br /> | '''CATHEPSIN D AT PH 7.5'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LYW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with EPE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cathepsin_D Cathepsin D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.5 3.4.23.5] Full crystallographic information is available from [http:// | + | 1LYW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cathepsin_D Cathepsin D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.5 3.4.23.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:21:17 2008'' |
Revision as of 14:21, 15 February 2008
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CATHEPSIN D AT PH 7.5
Contents |
Overview
The crystal structure of a catalytically inactive form of cathepsin D, (CatDhi) has been obtained at pH 7.5. The N-terminal strand relocates by, 30 A from its position in the interdomain beta-sheet and inserts into the, active site cleft, effectively blocking substrate access. CatDhi has a, five-stranded interdomain beta-sheet and resembles Intermediate 3, a, hypothetical structure proposed to be transiently formed during, proteolytic activation of the proenzyme precursor. Interconversion between, active and inactive forms of CatD is reversible and may be regulated by an, ionizable switch involving the carboxylate side chains of Glu 5, Glu 180, and Asp 187. Our findings provide a structural basis for the pH-dependent, regulation of aspartic proteinase activity and suggest a novel mechanism, for pH-dependent modulation of substrate specificity.
Disease
Known diseases associated with this structure: Ceroid lipofuscinosis, neuronal, 10 OMIM:[116840]
About this Structure
1LYW is a Protein complex structure of sequences from Homo sapiens with as ligand. Active as Cathepsin D, with EC number 3.4.23.5 Full crystallographic information is available from OCA.
Reference
Conformational switching in an aspartic proteinase., Lee AY, Gulnik SV, Erickson JW, Nat Struct Biol. 1998 Oct;5(10):866-71. PMID:9783744
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