4d6a

Human myelin protein P2 after neutron scattering experiments

spinqualitylabelsall models 4d6a, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d6a is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: CIT, CSO, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYP2_HUMAN May play a role in lipid transport protein in Schwann cells. May bind cholesterol. Publication Abstract from PubMed Myelin protein P2 is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system, and its function is related to its membrane binding capacity. Here, the link between P2 protein dynamics and structure and function was studied using elastic incoherent neutron scattering (EINS). The P38G mutation, at the hinge between the beta barrel and the alpha-helical lid, increased the lipid stacking capacity of human P2 in vitro, and the mutated protein was also functional in cultured cells. The P38G mutation did not change the overall structure of the protein. For a deeper insight into P2 structure-function relationships, information on protein dynamics in the 10 ps to 1 ns time scale was obtained using EINS. Values of mean square displacements mainly from protein H atoms were extracted for wild-type P2 and the P38G mutant and compared. Our results show that at physiological temperatures, the P38G mutant is more dynamic than the wild-type P2 protein, especially on a slow 1-ns time scale. Molecular dynamics simulations confirmed the enhanced dynamics of the mutant variant, especially within the portal region in the presence of bound fatty acid. The increased softness of the hinge mutant of human myelin P2 protein is likely related to an enhanced flexibility of the portal region of this fatty acid-binding protein, as well as to its interactions with the lipid bilayer surface requiring conformational adaptations. Dynamics of the Peripheral Membrane Protein P2 from Human Myelin Measured by Neutron Scattering-A Comparison between Wild-Type Protein and a Hinge Mutant.,Laulumaa S, Nieminen T, Lehtimaki M, Aggarwal S, Simons M, Koza MM, Vattulainen I, Kursula P, Natali F PLoS One. 2015 Jun 11;10(6):e0128954. doi: 10.1371/journal.pone.0128954., eCollection 2015. PMID:26068118 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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