This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1yp8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:31, 6 December 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1yp8.gif|left|200px]]
 
-
{{Structure
+
==Solution structure of the cyclotide tricyclon A==
-
|PDB= 1yp8 |SIZE=350|CAPTION= <scene name='initialview01'>1yp8</scene>
+
<StructureSection load='1yp8' size='340' side='right'caption='[[1yp8]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<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>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yp8 OCA], [http://www.ebi.ac.uk/pdbsum/1yp8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yp8 RCSB]</span>
+
[https://www.uniprot.org/uniprot/TRIC_VIOAR TRIC_VIOAR]
-
}}
+
<div style="background-color:#fffaf0;">
-
 
+
== Publication Abstract from PubMed ==
-
'''Solution structure of the cyclotide tricyclon A'''
+
-
 
+
-
 
+
-
==Overview==
+
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.
-
==About this Structure==
+
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>
-
1YP8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Viola_tricolor Viola tricolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YP8 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</div>
-
[[Category: Protein complex]]
+
<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, D J.]]
+
[[Category: Craik DJ]]
-
[[Category: Mulvenna, J P.]]
+
[[Category: Mulvenna JP]]
-
[[Category: Sando, L.]]
+
[[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 Mar 31 01:16:27 2008''
+

Current revision

Solution structure of the cyclotide tricyclon A

PDB ID 1yp8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yp8"
Personal tools