2fo5

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[[Image:2fo5.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2fo5| PDB=2fo5 | SCENE= }}
{{STRUCTURE_2fo5| PDB=2fo5 | SCENE= }}
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'''Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin'''
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===Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin===
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==Overview==
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We describe the heterologous expression in Escherichia coli of the proenzyme precursor to EP-B2, a cysteine endoprotease from germinating barley seeds. High yields (50 mg/l) of recombinant proEP-B2 were obtained from E. coli inclusion bodies in shake flask cultures following purification and refolding. The zymogen was rapidly autoactivated to its mature form under acidic conditions at a rate independent of proEP-B2 concentration, suggesting a cis mechanism of autoactivation. Mature EP-B2 was stable and active over a wide pH range and efficiently hydrolyzed a recombinant wheat gluten protein, alpha2-gliadin, at sequences with known immunotoxicity in celiac sprue patients. The X-ray crystal structure of mature EP-B2 bound to leupeptin was solved to 2.2 A resolution and provided atomic insights into the observed subsite specificity of the endoprotease. Our findings suggest that orally administered proEP-B2 may be especially well suited for treatment of celiac sprue.
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(as it appears on PubMed at http://www.pubmed.gov), where 16793521 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16793521}}
==About this Structure==
==About this Structure==
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[[Category: Epb2]]
[[Category: Epb2]]
[[Category: Leupeptin]]
[[Category: Leupeptin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:07:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:45:06 2008''

Revision as of 16:45, 27 July 2008

Template:STRUCTURE 2fo5

Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin

Template:ABSTRACT PUBMED 16793521

About this Structure

2FO5 is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.

Reference

Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease., Bethune MT, Strop P, Tang Y, Sollid LM, Khosla C, Chem Biol. 2006 Jun;13(6):637-47. PMID:16793521

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