6CXP
HRFLRH peptide NMR structure in the presence of Cd(II)
Summary for 6CXP
| Entry DOI | 10.2210/pdb6cxp/pdb |
| NMR Information | BMRB: 30447 |
| Descriptor | Hexapeptide HRFLRH (1 entity in total) |
| Functional Keywords | amphibian skin secretion, metal affinity, co2 affinity, metal binding protein |
| Biological source | Phyllomedusa centralis (Mato Grosso leaf frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 867.04 |
| Authors | Pires, D.A.T.,Arake, L.M.R.,Silva, L.P.,Lopez-Castillo, A.,Prates, M.V.,Nascimento, C.J.,Bloch Jr, C. (deposition date: 2018-04-03, release date: 2018-07-04, Last modification date: 2024-05-15) |
| Primary citation | Pires, D.A.T.,Arake, L.M.R.,Silva, L.P.,Lopez-Castillo, A.,Prates, M.V.,Nascimento, C.J.,Bloch, C. A previously undescribed hexapeptide His-Arg-Phe-Leu-Arg-His-NH2from amphibian skin secretion shows CO2and metal biding affinities. Peptides, 106:37-44, 2018 Cited by PubMed Abstract: A previously undescribed six residues long peptide His-Arg-Phe-Leu-Arg-His was identified and purified from the skin secretion of the amphibian Phyllomedusa centralis. A synthetic analogue carboxyamidated HRFLRH-NH showed structural changes induced by CO and metal ions in aqueous solution when analyzed by NMR. The present work reports NMR structures for the carboxyamidated hexapeptide in the presence CO, Zn and Cd, suggesting possible affinity regions on the polypeptide chain for each ligand. The NMR structures were optimized by DFT to identify probable biding sites of these species in the polypeptide structure. To our best knowledge, this is the first time that a putative CO binding site is described on a peptide structure obtained in aqueous conditions, at room temperature. PubMed: 29933027DOI: 10.1016/j.peptides.2018.06.003 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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