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| - | [[Image:1y1b.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1y1b| PDB=1y1b | SCENE= }} | | {{STRUCTURE_1y1b| PDB=1y1b | SCENE= }} |
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| - | '''Solution structure of Anemonia elastase inhibitor'''
| + | ===Solution structure of Anemonia elastase inhibitor=== |
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| - | ==Overview==
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| - | Anemonia elastase inhibitor (AEI) is a "nonclassical" Kazal-type elastase inhibitor from Anemonia sulcata. Unlike many nonclassical inhibitors, AEI does not have a cystine-stabilized alpha-helical (CSH) motif in the sequence. We chemically synthesized AEI and determined its three-dimensional solution structure by two-dimensional NMR spectroscopy. The resulting structure of AEI was characterized by a central alpha-helix and a three-stranded antiparallel beta-sheet of a typical Kazal-type inhibitor such as silver pheasant ovomucoid third domain (OMSVP3), even though the first and fifth half-cystine residues forming a disulfide bond in AEI are shifted both toward the C-terminus in comparison with those of OMSVP3. Synthesized AEI exhibited unexpected strong inhibition toward Streptomyces griseus protease B (SGPB). Our previous study [Hemmi, H., et al. (2003) Biochemistry 42, 2524-2534] demonstrated that the site-specific introduction of the engineered disulfide bond into the OMSVP3 molecule to form the CSH motif could produce an inhibitor with a narrower specificity. Thus, the CSH motif-containing derivative of AEI (AEI analogue) was chemically synthesized when a Cys(4)-Cys(34) bond was changed to a Cys(6)-Cys(31) bond. The AEI analogue scarcely inhibited porcine pancreatic elastase (PPE), even though it exhibited almost the same potent inhibitory activity toward SGPB. For the molecular scaffold, essentially no structural difference was detected between the two, but the N-terminal loop from Pro(5) to Ile(7) near the putative reactive site (Met(10)-Gln(11)) in the analogue moved by 3.7 A toward the central helix to form the introduced Cys(6)-Cys(31) bond. Such a conformational change in the restricted region correlates with the specificity change of the inhibitor.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16008348}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16008348 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16008348}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1Y1B is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1B OCA]. | + | 1Y1B is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y1B OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Non-classical]] | | [[Category: Non-classical]] |
| | [[Category: Protease inhibitor]] | | [[Category: Protease inhibitor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:45:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:04:47 2008'' |
Revision as of 00:04, 29 July 2008
Template:STRUCTURE 1y1b
Solution structure of Anemonia elastase inhibitor
Template:ABSTRACT PUBMED 16008348
About this Structure
1Y1B is a Single protein structure. Full experimental information is available from OCA.
Reference
Structural and functional study of an Anemonia elastase inhibitor, a "nonclassical" Kazal-type inhibitor from Anemonia sulcata., Hemmi H, Kumazaki T, Yoshizawa-Kumagaye K, Nishiuchi Y, Yoshida T, Ohkubo T, Kobayashi Y, Biochemistry. 2005 Jul 19;44(28):9626-36. PMID:16008348
Page seeded by OCA on Tue Jul 29 03:04:47 2008
