1qh2: Difference between revisions

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[[Image:1qh2.jpg|left|200px]]


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==CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA==
The line below this paragraph, containing "STRUCTURE_1qh2", creates the "Structure Box" on the page.
<StructureSection load='1qh2' size='340' side='right'caption='[[1qh2]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1qh2|  PDB=1qh2  |  SCENE= }}
</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.


'''CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qh2" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
 
== References ==
==About this Structure==
<references/>
1QH2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Nicotiana_alata Nicotiana alata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH2 OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/10360353 10360353]
[[Category: Nicotiana alata]]
[[Category: Protein complex]]
[[Category: Anderson, M A.]]
[[Category: Craik, D J.]]
[[Category: Lee, M C.S.]]
[[Category: Scanlon, M J.]]
[[Category: Nicotiana alata]]
[[Category: Nicotiana alata]]
[[Category: Potato ii trypsin inhibitor]]
[[Category: Anderson MA]]
[[Category: Serine proteinase inhibitor]]
[[Category: Craik DJ]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:15:48 2008''
[[Category: Lee MCS]]
[[Category: Scanlon MJ]]

Latest revision as of 12:19, 6 December 2023

CHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATACHYMOTRYPSIN INHIBITOR (C2) FROM NICOTIANA ALATA

Structural highlights

1qh2 is a 2 chain structure with sequence from Nicotiana alata. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q40378_NICAL

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Lee MC, Scanlon MJ, Craik DJ, Anderson MA. A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein. Nat Struct Biol. 1999 Jun;6(6):526-30. PMID:10360353 doi:10.1038/9293
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