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6EW5

Human myelin protein P2 F57A mutant, monoclinic crystal form

Summary for 6EW5
Entry DOI10.2210/pdb6ew5/pdb
Related6EW2 6EW4
DescriptorMyelin P2 protein, PALMITIC ACID (3 entities in total)
Functional Keywordsfatty acid binding protein, beta barrel, portal region, lipid transport
Biological sourceHomo sapiens (Human)
Total number of polymer chains4
Total formula weight60687.19
Authors
Laulumaa, S.,Lehtimaki, M.,Kursula, P. (deposition date: 2017-11-03, release date: 2018-07-11, Last modification date: 2024-10-23)
Primary citationLaulumaa, 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: 29940944
DOI: 10.1186/s12900-018-0087-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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数据于2024-11-13公开中

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