4W6V

Crystal structure of a peptide transporter from Yersinia enterocolitica at 3 A resolution

4W6V の概要

• エントリーDOI: 10.2210/pdb4w6v/pdb
• 分子名称: Di-/tripeptide transporter (1 entity in total)
• 機能のキーワード: membrane protein, transport protein, solute transporter, permease
• 由来する生物種: Yersinia enterocolitica subsp. palearctica YE-P4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56509.90

構造登録者

Jeckelmann, J.-M.,Boggavarapu, R.,Harder, D.,Ucurum, Z.,Fotiadis, D. (登録日: 2014-08-21, 公開日: 2015-07-15, 最終更新日: 2024-01-10)

主引用文献

Boggavarapu, R.,Jeckelmann, J.M.,Harder, D.,Ucurum, Z.,Fotiadis, D.
Role of electrostatic interactions for ligand recognition and specificity of peptide transporters.
Bmc Biol., 13:58-58, 2015

PubMed Abstract: Peptide transporters are membrane proteins that mediate the cellular uptake of di- and tripeptides, and of peptidomimetic drugs such as β-lactam antibiotics, antiviral drugs and antineoplastic agents. In spite of their high physiological and pharmaceutical importance, the molecular recognition by these transporters of the amino acid side chains of short peptides and thus the mechanisms for substrate binding and specificity are far from being understood.

PubMed: 26246134
DOI: 10.1186/s12915-015-0167-8

実験手法

X-RAY DIFFRACTION (3.01819 Å)