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Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins

Overview of attention for article published in BMC Structural Biology, June 2018
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Title
Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins
Published in
BMC Structural Biology, June 2018
DOI 10.1186/s12900-018-0087-2
Pubmed ID
Authors

Saara Laulumaa, Tuomo Nieminen, Arne Raasakka, Oda C. Krokengen, Anushik Safaryan, Erik I. Hallin, Guillaume Brysbaert, Marc F. Lensink, Salla Ruskamo, Ilpo Vattulainen, Petri Kursula

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. We performed a structural characterization of the F57A mutant of human P2. The mutant protein was crystallized in three crystal forms, all of which showed changes in the portal region and helix α2. In addition, the behaviour of the mutant protein upon lipid bilayer binding suggested more unfolding than previously observed for wild-type P2. On the other hand, membrane binding rendered F57A heat-stable, similarly to wild-type P2. Atomistic molecular dynamics simulations showed opening of the side of the discontinuous β barrel, giving important indications on the mechanism of portal region opening and ligand entry into FABPs. The results suggest a central role for Phe57 in regulating the opening of the portal region in human P2 and other FABPs, and the F57A mutation disturbs dynamic cross-correlation networks in the portal region of P2. Overall, the F57A variant presents similar properties to the P2 patient mutations recently linked to Charcot-Marie-Tooth disease. Our results identify Phe57 as a residue regulating conformational changes that may accompany membrane surface binding and ligand exchange in P2 and other FABPs.

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Mendeley readers

The data shown below were compiled from readership statistics for 22 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 22 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 4 18%
Student > Doctoral Student 3 14%
Student > Bachelor 3 14%
Other 2 9%
Professor > Associate Professor 2 9%
Other 3 14%
Unknown 5 23%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 9 41%
Agricultural and Biological Sciences 2 9%
Business, Management and Accounting 1 5%
Psychology 1 5%
Neuroscience 1 5%
Other 1 5%
Unknown 7 32%

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 02 August 2018.
All research outputs
#13,398,850
of 20,760,702 outputs
Outputs from BMC Structural Biology
#123
of 212 outputs
Outputs of similar age
#174,410
of 296,267 outputs
Outputs of similar age from BMC Structural Biology
#1
of 1 outputs
Altmetric has tracked 20,760,702 research outputs across all sources so far. This one is in the 33rd percentile – i.e., 33% of other outputs scored the same or lower than it.
So far Altmetric has tracked 212 research outputs from this source. They receive a mean Attention Score of 3.2. This one is in the 40th percentile – i.e., 40% of its peers scored the same or lower than it.
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