6CXQ

HRFLRH peptide NMR structure in the presence of CO2

6CXQ の概要

• エントリーDOI: 10.2210/pdb6cxq/pdb
• NMR情報: BMRB: 30448
• 分子名称: Hexapeptide HRFLRH (1 entity in total)
• 機能のキーワード: amphibian skin secretion, metal affinity, co2 affinity, metal binding protein
• 由来する生物種: Phyllomedusa centralis (Mato Grosso leaf frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 867.04

構造登録者

Pires, D.A.T.,Arake, L.M.R.,Silva, L.P.,Lopez-Castillo, A.,Prates, M.V.,Nascimento, C.J.,Bloch Jr, C. (登録日: 2018-04-03, 公開日: 2018-07-04, 最終更新日: 2024-10-09)

主引用文献

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

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: 29933027
DOI: 10.1016/j.peptides.2018.06.003

実験手法

SOLUTION NMR