1yp8

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(New page: 200px<br /><applet load="1yp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yp8" /> '''Solution structure of the cyclotide tricyclo...)
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[[Image:1yp8.gif|left|200px]]<br /><applet load="1yp8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yp8" />
 
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'''Solution structure of the cyclotide tricyclon A'''<br />
 
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==Overview==
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==Solution structure of the cyclotide tricyclon A==
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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.
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<StructureSection load='1yp8' size='340' side='right'caption='[[1yp8]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRIC_VIOAR TRIC_VIOAR]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1YP8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Viola_tricolor Viola tricolor]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YP8 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15893660 15893660]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1yp8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Viola tricolor]]
[[Category: Viola tricolor]]
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[[Category: Craik, D.J.]]
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[[Category: Craik DJ]]
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[[Category: Mulvenna, J.P.]]
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[[Category: Mulvenna JP]]
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[[Category: Sando, L.]]
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[[Category: Sando L]]
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[[Category: beta-sheet]]
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[[Category: cyclic backbone]]
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[[Category: cyclotide]]
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[[Category: cystine knot]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:57:46 2007''
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Current revision

Solution structure of the cyclotide tricyclon A

PDB ID 1yp8

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