SASDAS3: Fila16-17 (immunoglobulin- like filamin two-domain fragment 16-17)

Basic information

• Entry: Database: SASBDB / ID: SASDAS3

Sample

Fila16-17

• immunoglobulin- like filamin two-domain fragment 16-17 (protein), Fila16-17, Escherichia coli

• Biological species: Escherichia coli (E. coli)
• Citation: Journal: J Biol Chem / Year: 2009; Title: Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin.; Authors: Outi K Heikkinen / Salla Ruskamo / Peter V Konarev / Dmitri I Svergun / Tatu Iivanainen / Sami M Heikkinen / Perttu Permi / Harri Koskela / Ilkka Kilpeläinen / Jari Ylänne / ; Abstract: Filamins are actin filament cross-linking proteins composed of an N-terminal actin-binding domain and 24 immunoglobulin-like domains (IgFLNs). Filamins interact with numerous proteins, including the cytoplasmic domains of plasma membrane signaling and cell adhesion receptors. Thereby filamins mechanically and functionally link the cell membrane to the cytoskeleton. Most of the interactions have been mapped to the C-terminal IgFLNs 16-24. Similarly, as with the previously known compact domain pair of IgFLNa20-21, the two-domain fragments IgFLNa16-17 and IgFLNa18-19 were more compact in small angle x-ray scattering analysis than would be expected for two independent domains. Solution state NMR structures revealed that the domain packing in IgFLNa18-19 resembles the structure of IgFLNa20-21. In both domain pairs the integrin-binding site is masked, although the details of the domain-domain interaction are partly distinct. The structure of IgFLNa16-17 revealed a new domain packing mode where the adhesion receptor binding site of domain 17 is not masked. Sequence comparison suggests that similar packing of three tandem filamin domain pairs is present throughout the animal kingdom, and we propose that this packing is involved in the regulation of filamin interactions through a mechanosensor mechanism.

Contact author

• Petr Konarev (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

Models

• Model #37: ; Type: dummy / Software: Gasbor and Damaver / Chi-square value: 2.8561; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Fila16-17 / Sample MW: 18.7 kDa
• Buffer: Name: 100 mM NaCl, 10 mM dithiothreitol, 20 mM Tris / pH: 8

Entity #34

Name: Fila16-17 / Type: protein
Description: immunoglobulin- like filamin two-domain fragment 16-17
Formula weight: 18.7 / Num. of mol.: 1 / Source: Escherichia coli
Sequence:

GRVKESITRR RRAPSVANVG SHCDLSIQDM TAQVTSPSGK THEAECIRFV PAEMGTHTVS VKYKGQHVPG SPFQFTVGPL GEGGAHKVRA GGPGLERAEA GVPAEFSIWT REAGAGGLAI AVEGPSKAEI SFEDRKDGSC GVAYVVQEPG DYEVSVKFNE EHIPDSPFVV PVASP

Experimental information

• Beam: Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron
• Detector: Name: MAR 345 Image Plate

Scan

Title: Fila16-17 / Measurement date: Jun 18, 2007 / Storage temperature: 10 °C / Cell temperature: 10 °C / Unit: 1/nm /

	Min	Max
Q	0.1354	3.5391

Distance distribution function P(R)

Sofotware P(R): GNOM 4.5a / Number of points: 490 /

	Min	Max
Q	0.1377	3.537
P(R) point	1	490
R	0	6

Result

D max: 6 / Type of curve: single_conc / Standard: BSA /

	Experimental	Porod	Estimated
MW	22 kDa	-	-
Volume	-	33 nm3	32

	P(R)	Guinier
Forward scattering, I0	41.6	41.5
Radius of gyration, Rg	1.93 nm	1.92 nm