Solution structure of the C-terminally encoded peptide of the plant parasitic nematode Meloidogyne hapla - CEP11Solution structure of the C-terminally encoded peptide of the plant parasitic nematode Meloidogyne hapla - CEP11

Structural highlights

2mfm is a 1 chain structure with sequence from Meloidogyne hapla. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G7K427_MEDTR

Publication Abstract from PubMed

The C-terminally Encoded Peptide (CEP) family of regulatory peptides controls root development in vascular plants. Here, we present the first NMR structures of CEP. We show that root-knot nematode (RKN: Meloidogyne spp.) also encodes CEP, presumably to mimic plant CEP as part of their stereotypic, parasitic interaction with vascular plants. Molecular dynamics simulations of plant- and nematode-encoded CEP displaying known posttranslational modifications (PTM) provided insight into the structural effects of PTM and the conformational plasticity and rigidity of CEP. Potential mechanisms of action are discussed with respect to the structure and sampling of conformational space.

Solution NMR studies of the plant peptide hormone CEP inform function.,Bobay BG, Digennaro P, Scholl E, Imin N, Djordjevic MA, McK Bird D FEBS Lett. 2013 Dec 11;587(24):3979-85. doi: 10.1016/j.febslet.2013.10.033. Epub , 2013 Nov 5. PMID:24211833[1]

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

References

  1. Bobay BG, Digennaro P, Scholl E, Imin N, Djordjevic MA, McK Bird D. Solution NMR studies of the plant peptide hormone CEP inform function. FEBS Lett. 2013 Dec 11;587(24):3979-85. doi: 10.1016/j.febslet.2013.10.033. Epub , 2013 Nov 5. PMID:24211833 doi:http://dx.doi.org/10.1016/j.febslet.2013.10.033
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