1yp8: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (13 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Solution structure of the cyclotide tricyclon A== | ||
<StructureSection load='1yp8' size='340' side='right'caption='[[1yp8]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
</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. | 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<ref>PMID:15893660</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1yp8" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Viola tricolor]] | [[Category: Viola tricolor]] | ||
[[Category: Craik | [[Category: Craik DJ]] | ||
[[Category: Mulvenna | [[Category: Mulvenna JP]] | ||
[[Category: Sando | [[Category: Sando L]] | ||
Latest revision as of 10:32, 9 October 2024
Solution structure of the cyclotide tricyclon ASolution structure of the cyclotide tricyclon A
Structural highlights
FunctionPublication Abstract from PubMedCyclotides 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
|
| ||||||||||||||||