1yp8: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1yp8.png|left|200px]]


<!--
==Solution structure of the cyclotide tricyclon A==
The line below this paragraph, containing "STRUCTURE_1yp8", creates the "Structure Box" on the page.
<StructureSection load='1yp8' size='340' side='right'caption='[[1yp8]]' 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'>[[1yp8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Viola_tricolor Viola tricolor]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YP8 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, 20 models</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=1yp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yp8 OCA], [https://pdbe.org/1yp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yp8 RCSB], [https://www.ebi.ac.uk/pdbsum/1yp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yp8 ProSAT]</span></td></tr>
{{STRUCTURE_1yp8|  PDB=1yp8  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRIC_VIOAR TRIC_VIOAR]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cyclotides are a family of plant proteins that have the unusual combination of head-to-tail backbone cyclization and a cystine knot motif. They are exceptionally stable and show resistance to most chemical, physical, and enzymatic treatments. The structure of tricyclon A, a previously unreported cyclotide, is described here. In this structure, a loop that is disordered in other cyclotides forms a beta sheet that protrudes from the globular core. This study indicates that the cyclotide fold is amenable to the introduction of a range of structural elements without affecting the cystine knot core of the protein, which is essential for the stability of the cyclotides. Tricyclon A does not possess a hydrophobic patch, typical of other cyclotides, and has minimal hemolytic activity, making it suitable for pharmaceutical applications. The 22 kDa precursor protein of tricyclon A was identified and provides clues to the processing of these fascinating miniproteins.


===Solution structure of the cyclotide tricyclon A===
Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A.,Mulvenna JP, Sando L, Craik DJ Structure. 2005 May;13(5):691-701. PMID:15893660<ref>PMID:15893660</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_15893660}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1yp8" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 15893660 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_15893660}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YP8 OCA].
[[Category: Viola tricolor]]
 
[[Category: Craik DJ]]
==Reference==
[[Category: Mulvenna JP]]
Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A., Mulvenna JP, Sando L, Craik DJ, Structure. 2005 May;13(5):691-701. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15893660 15893660]
[[Category: Sando L]]
[[Category: Craik, D J.]]
[[Category: Mulvenna, J P.]]
[[Category: Sando, L.]]
[[Category: Beta-sheet]]
[[Category: Cyclic backbone]]
[[Category: Cyclotide]]
[[Category: Cystine knot]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:03:45 2008''

Latest revision as of 10:32, 9 October 2024

Solution structure of the cyclotide tricyclon ASolution structure of the cyclotide tricyclon A

Structural highlights

1yp8 is a 1 chain structure with sequence from Viola tricolor. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRIC_VIOAR

Publication Abstract from PubMed

Cyclotides are a family of plant proteins that have the unusual combination of head-to-tail backbone cyclization and a cystine knot motif. They are exceptionally stable and show resistance to most chemical, physical, and enzymatic treatments. The structure of tricyclon A, a previously unreported cyclotide, is described here. In this structure, a loop that is disordered in other cyclotides forms a beta sheet that protrudes from the globular core. This study indicates that the cyclotide fold is amenable to the introduction of a range of structural elements without affecting the cystine knot core of the protein, which is essential for the stability of the cyclotides. Tricyclon A does not possess a hydrophobic patch, typical of other cyclotides, and has minimal hemolytic activity, making it suitable for pharmaceutical applications. The 22 kDa precursor protein of tricyclon A was identified and provides clues to the processing of these fascinating miniproteins.

Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A.,Mulvenna JP, Sando L, Craik DJ Structure. 2005 May;13(5):691-701. PMID:15893660[1]

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

References

  1. ↑ Mulvenna JP, Sando L, Craik DJ. Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A. Structure. 2005 May;13(5):691-701. PMID:15893660 doi:S0969-2126(05)00117-6
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1yp8&oldid=4185245"