1wn4
From Proteopedia
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- | [[Image:1wn4.jpg|left|200px]] | + | [[Image:1wn4.jpg|left|200px]] |
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- | '''NMR Structure of VoNTR''' | + | {{Structure |
+ | |PDB= 1wn4 |SIZE=350|CAPTION= <scene name='initialview01'>1wn4</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''NMR Structure of VoNTR''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1WN4 is a [ | + | 1WN4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WN4 OCA]. |
==Reference== | ==Reference== | ||
- | Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins., Dutton JL, Renda RF, Waine C, Clark RJ, Daly NL, Jennings CV, Anderson MA, Craik DJ, J Biol Chem. 2004 Nov 5;279(45):46858-67. Epub 2004 Aug 24. PMID:[http:// | + | Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins., Dutton JL, Renda RF, Waine C, Clark RJ, Daly NL, Jennings CV, Anderson MA, Craik DJ, J Biol Chem. 2004 Nov 5;279(45):46858-67. Epub 2004 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15328347 15328347] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Anderson, M A.]] | [[Category: Anderson, M A.]] | ||
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[[Category: helix]] | [[Category: helix]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:59:11 2008'' |
Revision as of 12:59, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
NMR Structure of VoNTR
Overview
The cyclotides are the largest family of naturally occurring circular proteins. The mechanism by which the termini of these gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding cDNA sequences from the plant Viola odorata and compare them with those from an evolutionarily distinct species, Oldenlandia affinis. Individual members of this multigene family encode one to three mature cyclotide domains. These domains are preceded by N-terminal repeat regions (NTRs) that are conserved within a plant species but not between species. We have structurally characterized peptides corresponding to these NTRs and show that, despite them having no sequence homology, they form a structurally conserved alpha-helical motif. This structural conservation suggests a vital role for the NTR in the in vivo folding, processing, or detoxification of cyclotide domains from the precursor protein.
About this Structure
1WN4 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins., Dutton JL, Renda RF, Waine C, Clark RJ, Daly NL, Jennings CV, Anderson MA, Craik DJ, J Biol Chem. 2004 Nov 5;279(45):46858-67. Epub 2004 Aug 24. PMID:15328347
Page seeded by OCA on Thu Mar 20 14:59:11 2008