6EW5

Human myelin protein P2 F57A mutant, monoclinic crystal form

6EW5 の概要

• エントリーDOI: 10.2210/pdb6ew5/pdb
• 関連するPDBエントリー: 6EW2 6EW4
• 分子名称: Myelin P2 protein, PALMITIC ACID (3 entities in total)
• 機能のキーワード: fatty acid binding protein, beta barrel, portal region, lipid transport
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 60687.19

構造登録者

Laulumaa, S.,Lehtimaki, M.,Kursula, P. (登録日: 2017-11-03, 公開日: 2018-07-11, 最終更新日: 2024-10-23)

主引用文献

Laulumaa, S.,Nieminen, T.,Raasakka, A.,Krokengen, O.C.,Safaryan, A.,Hallin, E.I.,Brysbaert, G.,Lensink, M.F.,Ruskamo, S.,Vattulainen, I.,Kursula, P.
Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the beta barrel in fatty acid binding proteins.
BMC Struct. Biol., 18:8-8, 2018

PubMed Abstract: Myelin is a multilayered proteolipid sheath wrapped around selected axons in the nervous system. Its constituent proteins play major roles in forming of the highly regular membrane structure. P2 is a myelin-specific protein of the fatty acid binding protein (FABP) superfamily, which is able to stack lipid bilayers together, and it is a target for mutations in the human inherited neuropathy Charcot-Marie-Tooth disease. A conserved residue that has been proposed to participate in membrane and fatty acid binding and conformational changes in FABPs is Phe57. This residue is thought to be a gatekeeper for the opening of the portal region upon ligand entry and egress.

PubMed: 29940944
DOI: 10.1186/s12900-018-0087-2

実験手法

X-RAY DIFFRACTION (1.95 Å)