4BVM

The peripheral membrane protein P2 from human myelin at atomic resolution

4BVM の概要

• エントリーDOI: 10.2210/pdb4bvm/pdb
• 分子名称: MYELIN P2 PROTEIN, PALMITIC ACID, VACCENIC ACID, ... (5 entities in total)
• 機能のキーワード: membrane protein, fabp, ultrahigh resolution
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm : P02689
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15914.60

構造登録者

Ruskamo, S.,Yadav, R.P.,Kursula, P. (登録日: 2013-06-26, 公開日: 2014-01-15, 最終更新日: 2023-12-20)

主引用文献

Ruskamo, S.,Yadav, R.P.,Sharma, S.,Lehtimaki, M.,Laulumaa, S.,Aggarwal, S.,Simons, M.,Burck, J.,Ulrich, A.S.,Juffer, A.H.,Kursula, I.,Kursula, P.
Atomic Resolution View Into the Structure-Function Relationships of the Human Myelin Peripheral Membrane Protein P2
Acta Crystallogr.,Sect.D, 70:165-, 2014

PubMed Abstract: P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 Å allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation of the bound fatty-acid carboxyl group is linked to the protonation states of two coordinating arginine residues. An anion-binding site in the portal region is suggested to be relevant for membrane interactions and conformational changes. When bound to membrane multilayers, P2 has a preferred orientation and is stabilized, and the repeat distance indicates a single layer of P2 between membranes. Simulations show the formation of a double bilayer in the presence of P2, and in cultured cells wild-type P2 induces membrane-domain formation. Here, the most accurate structural and functional view to date on P2, a major component of peripheral nerve myelin, is presented, showing how it can interact with two membranes simultaneously while going through conformational changes at its portal region enabling ligand transfer.

PubMed: 24419389
DOI: 10.1107/S1399004713027910

実験手法

X-RAY DIFFRACTION (0.93 Å)