6EW2
Human myelin protein P2 F57A mutant, tetragonal crystal form
Summary for 6EW2
| Entry DOI | 10.2210/pdb6ew2/pdb |
| Descriptor | Myelin P2 protein, PALMITIC ACID, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | fatty acid binding protein, beta barrel, portal region, lipid transport |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15207.25 |
| Authors | Laulumaa, S.,Lehtimaki, M.,Kursula, P. (deposition date: 2017-11-03, release date: 2018-07-11, Last modification date: 2024-10-23) |
| Primary citation | 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 Cited by 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: 29940944DOI: 10.1186/s12900-018-0087-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.588 Å) |
Structure validation
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