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New page: left|200px<br /><applet load="1qh2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qh2" /> '''CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA A... |
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== | ==CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA== | ||
Female reproductive tissues of the ornamental tobacco amass high levels of | <StructureSection load='1qh2' size='340' side='right'caption='[[1qh2]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1qh2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_alata Nicotiana alata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QH2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qh2 OCA], [https://pdbe.org/1qh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qh2 RCSB], [https://www.ebi.ac.uk/pdbsum/1qh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qh2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q40378_NICAL Q40378_NICAL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Female reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family. | |||
A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein.,Lee MC, Scanlon MJ, Craik DJ, Anderson MA Nat Struct Biol. 1999 Jun;6(6):526-30. PMID:10360353<ref>PMID:10360353</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1qh2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Nicotiana alata]] | [[Category: Nicotiana alata]] | ||
[[Category: Anderson MA]] | |||
[[Category: Anderson | [[Category: Craik DJ]] | ||
[[Category: Craik | [[Category: Lee MCS]] | ||
[[Category: Lee | [[Category: Scanlon MJ]] | ||
[[Category: Scanlon | |||
Latest revision as of 12:19, 6 December 2023
CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATACHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA
Structural highlights
FunctionPublication Abstract from PubMedFemale reproductive tissues of the ornamental tobacco amass high levels of serine proteinase inhibitors (PIs) for protection against pests and pathogens. These PIs are produced from a precursor protein composed of six repeats each with a protease reactive site. Here we show that proteolytic processing of the precursor generates five single-chain PIs and a remarkable two-chain inhibitor formed by disulfide-bond linkage of N- and C-terminal peptide fragments. Surprisingly, PI precursors adopt this circular structure regardless of the number of inhibitor domains, suggesting this bracelet-like conformation is characteristic of the widespread potato inhibitor II (Pot II) protein family. A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein.,Lee MC, Scanlon MJ, Craik DJ, Anderson MA Nat Struct Biol. 1999 Jun;6(6):526-30. PMID:10360353[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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