3KFI

Major mouse urinary protein IV complexed with 2,5-dimethylpyrazine

3KFI の概要

• エントリーDOI: 10.2210/pdb3kfi/pdb
• 関連するPDBエントリー: 3KFF 3KFG 3KFH
• 分子名称: Major urinary protein 4, CHLORIDE ION, 2,5-dimethylpyrazine, ... (4 entities in total)
• 機能のキーワード: pheromone, major urinary protein, lipocalin, beta barrel, disulfide bond, pheromone-binding, secreted, transport, transport protein
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Secreted: P11590
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19025.48

構造登録者

Perez-Miller, S.,Zou, Q.,Hurley, T.D. (登録日: 2009-10-27, 公開日: 2010-06-16, 最終更新日: 2024-10-16)

主引用文献

Perez-Miller, S.,Zou, Q.,Novotny, M.V.,Hurley, T.D.
High resolution X-ray structures of mouse major urinary protein nasal isoform in complex with pheromones.
Protein Sci., 19:1469-1479, 2010

PubMed Abstract: In mice, the major urinary proteins (MUP) play a key role in pheromonal communication by binding and transporting semiochemicals. MUP-IV is the only isoform known to be expressed in the vomeronasal mucosa. In comparison with the MUP isoforms that are abundantly excreted in the urine, MUP-IV is highly specific for the male mouse pheromone 2-sec-butyl-4,5-dihydrothiazole (SBT). To examine the structural basis of this ligand preference, we determined the X-ray crystal structure of MUP-IV bound to three mouse pheromones: SBT, 2,5-dimethylpyrazine, and 2-heptanone. We also obtained the structure of MUP-IV with 2-ethylhexanol bound in the cavity. These four structures show that relative to the major excreted MUP isoforms, three amino acid substitutions within the binding calyx impact ligand coordination. The F103 for A along with F54 for L result in a smaller cavity, potentially creating a more closely packed environment for the ligand. The E118 for G substitution introduces a charged group into a hydrophobic environment. The sidechain of E118 is observed to hydrogen bond to polar groups on all four ligands with nearly the same geometry as seen for the water-mediated hydrogen bond network in the MUP-I and MUP-II crystal structures. These differences in cavity size and interactions between the protein and ligand are likely to contribute to the observed specificity of MUP-IV.

PubMed: 20509168
DOI: 10.1002/pro.426

実験手法

X-RAY DIFFRACTION (1.42 Å)