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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2007-5-8
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pubmed:abstractText |
The serpin endopin 2A inhibits the cysteine protease papain in cross-class inhibition. This study demonstrates the novel finding that both the non-RSL NH(2)-domain and the RSL domain with P1-P1' residues participate in endopin 2A inhibition. Production of a chimeric mutant of endopin 2A with replacement of its NH(2)-domain with that of endopin 1 resulted in less effective inhibition of papain, indicated by its lower k(ass) association rate constant compared to wild-type endopin 2A. This chimeric mutant formed complexes with papain, but at lower levels compared to that with wild-type endopin 2A. Papain degradation of a portion of the chimeric mutant suggested a role for the NH(2)-domain in regulating relative amounts of endopin 2A that enter the substrate pathway compared to the serpin inhibitory pathway. Furthermore, site-directed mutagenesis demonstrated that the RSL domain with intact P1-P1' residues was necessary for inhibition. These findings indicate that the NH(2)-domain and the RSL region both participate in endopin 2A inhibition of papain.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-01A10003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-01A19004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-020003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-029004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-030003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-039004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-040003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-049004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-04S10003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-04S19004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-050003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-059004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-06A10003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-06A19004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-070003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-079004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-080003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-089004,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-090003,
http://linkedlifedata.com/resource/pubmed/grant/P01 HL058120-099004,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-12,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-13,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-14,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-15,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-16,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-17,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-18,
http://linkedlifedata.com/resource/pubmed/grant/R01 NS024553-19
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-10567388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-10852705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-11821386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-11863458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-11939796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-12173926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-12475206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-12504904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-12809493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-15647007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-15649421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-15909990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-16716310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-2404007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-9548757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17451636-9811823
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
461
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
219-24
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:17451636-Animals,
pubmed-meshheading:17451636-Base Sequence,
pubmed-meshheading:17451636-Binding Sites,
pubmed-meshheading:17451636-Cattle,
pubmed-meshheading:17451636-Molecular Sequence Data,
pubmed-meshheading:17451636-Mutagenesis, Site-Directed,
pubmed-meshheading:17451636-Papain,
pubmed-meshheading:17451636-Protein Structure, Tertiary,
pubmed-meshheading:17451636-Serpins
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pubmed:year |
2007
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pubmed:articleTitle |
Multiple domains of endopin 2A for serpin cross-class inhibition of papain.
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pubmed:affiliation |
Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA 92093-0744, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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