Journal: PLoS One / Year: 2015 Title: Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. Authors: Jonne Seppälä / Helena Tossavainen / Nebojsa Rodic / Perttu Permi / Ulla Pentikäinen / Jari Ylänne / Abstract: Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix ...Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds for signaling proteins, and binding several other cytoskeletal proteins that regulate cell adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated that myosin-mediated contractile forces can reveal hidden protein binding sites in the domain pairs IgFLNa18-19 and 20-21, enabling FLNs to transduce mechanical signals in cells. The atomic structures of these mechanosensor domain pairs in the resting state are known, as well as the structures of individual IgFLN21 with ligand peptides. However, little experimental data is available on how interacting protein binding deforms the domain pair structures. Here, using small-angle x-ray scattering-based modelling, x-ray crystallography, and NMR, we show that the adaptor protein migfilin-derived peptide-bound structure of IgFLNa20-21 is flexible and adopts distinctive conformations depending on the presence or absence of the interacting peptide. The conformational changes reported here may be common for all peptides and may play a role in the mechanosensor function of the site.
Instrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.93 Å / Dist. spec. to detc.: 2.43 mm
Detector
Name: Pilatus 1M
Scan
Title: Human Filamin A Ig-like domains 20-21* / Measurement date: Feb 1, 2014 / Storage temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
Min
Max
Q
0.0937
4.63
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 416 /
Min
Max
Q
0.209
2.2
P(R) point
25
440
R
0
6.8
Result
Type of curve: merged Comments: Filamin A fragment residues 2141-2329 (Ig-like domains).
Experimental
Porod
MW
30 kDa
19 kDa
Volume
-
32 nm3
P(R)
P(R) error
Guinier
Forward scattering, I0
30
0.038
29.9
Radius of gyration, Rg
1.97 nm
-
1.9 nm
Min
Max
D
-
6.8
Guinier point
25
110
+
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Homo sapiens (human)
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/ Type of source: X-ray synchrotron / Wavelength: 0.93 Å / Dist. spec. to detc.: 2.43 mm
