4D5M

Gonadotropin-releasing hormone agonist

4D5M の概要

• エントリーDOI: 10.2210/pdb4d5m/pdb
• 分子名称: TRIPTORELIN, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: hormone, gnrh, lhrh, d-trp, decapeptide
• 由来する生物種: SYNTHETIC CONSTRUCT
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 5534.75

構造登録者

Legrand, P.,Le Du, M.-H.,Valery, C.,Deville-Foillard, S.,Paternostre, M.,Artzner, F. (登録日: 2014-11-05, 公開日: 2015-08-12, 最終更新日: 2024-10-16)

主引用文献

Valery, C.,Deville-Foillard, S.,Lefebvre, C.,Taberner, N.,Legrand, P.,Meneau, F.,Meriadec, C.,Delvaux, C.,Bizien, T.,Kasotakis, E.,Lopez-Iglesias, C.,Gall, A.,Bressanelli, S.,Le Du, M.-H.,Paternostre, M.,Artzner, F.
Atomic View of the Histidine Environment Stabilizing Higher- Ph Conformations of Ph-Dependent Proteins.
Nat.Commun., 6:7771-, 2015

PubMed Abstract: External stimuli are powerful tools that naturally control protein assemblies and functions. For example, during viral entry and exit changes in pH are known to trigger large protein conformational changes. However, the molecular features stabilizing the higher pH structures remain unclear. Here we elucidate the conformational change of a self-assembling peptide that forms either small or large nanotubes dependent on the pH. The sub-angstrom high-pH peptide structure reveals a globular conformation stabilized through a strong histidine-serine H-bond and a tight histidine-aromatic packing. Lowering the pH induces histidine protonation, disrupts these interactions and triggers a large change to an extended β-sheet-based conformation. Re-visiting available structures of proteins with pH-dependent conformations reveals both histidine-containing aromatic pockets and histidine-serine proximity as key motifs in higher pH structures. The mechanism discovered in this study may thus be generally used by pH-dependent proteins and opens new prospects in the field of nanomaterials.

PubMed: 26190377
DOI: 10.1038/NCOMMS8771

実験手法

X-RAY DIFFRACTION (0.85 Å)