Bioisis

"Interleukin (IL)-33 with primary receptor ST2"

Experimental SAS Curve

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Experimental Mass

58,300 Da

Experimental Details for BID:  ST2ILP
Experiment ID: 84
Collected at: NSRCC 23A, ALS BL 12.3.1
Contributors: Tainer, J ,  Hammel, M ,  Sali, A ,  Webb, B ,  Weinkam, P ,  Schneidman-duhovny, D
Interleukin (IL)-33 signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family. Combined crystallography and small-angle X-ray–scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution. The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
Various concentrations, 0.5-5mg/mL. At the NSRRC 23A beamline, 100 ?L of proteins in a sample cell were exposed for 30 and 60 s, and data was collected at wavelength ? = 0.8857 Å (energy, 14.000 KeV) with sample-to-detector distance 2.5 m, resulting in q

Electron Pair Distribution

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       Dmax → 100 Å


Guinier Plot

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     Guinier Rg → 28.85 Å

Real Space Rg → 30.44 Å

The Guinier plot is used to estimate the radius of gyration, Rg, which is taken from the slope of a line observed at low scattering angles (typically in the range where q* Rg < 1.3). This should be in reasonable agreement with the real space Rg.


Kratky Plot

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The Kratky plot can be used to visually assess the degree of "unfoldedness" of a protein or RNA sample. The plot of a well-behaved folded protein approaches the baseline at high q values creating a parabolic shape.


PDB Model fit to SAXS Data

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The red line is the calculated SAXS profile from a PDB model scaled to the experimental SAXS curve (cyan). The two curves agree with a Chi2 of 0.1.


Additional Experimental Details
Title

Interleukin (IL)-33 with primary receptor ST2

Description

Interleukin (IL)-33 signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family. Combined crystallography and small-angle X-ray–scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution. The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.

Publication

Structural insights into the interaction of IL-33 with its receptors, Proc Natl Acad Sci U S A. 2013 Sep 10;110(37):14918-23.

Contributors

Tainer, J ,  Hammel, M ,  Sali, A ,  Webb, B ,  Weinkam, P ,  Schneidman-duhovny, D

Genomics and Proteomics

The experiment is composed of 2 genes/ORFs

Abbreviated name: ST2

Annotation: 1 TIR domain; 3 Ig-like C2-type (immunoglobulin-like) domains

ADPKFSKQSW GLENEALIVR CPRQGKPSYT VDWYYSQTNK SIPTQERNRV FASGQLLKFL PAAVADSGIY TCIVRSPTFN RTGYANVTIY KKQSDCNVPD YLMYSTVSGS EKNSKIYCPT IDLYNWTAPL EWFKNCQALQ GSRYRAHKSF LVIDNVMTED AGDYTCKFIH NENGANYSVT ATRSFTVKDE QGFSLFPVIG APAQNEIKEV EIGKNANLTC SACFGKGTQF LAAVLWQLNG TKITDFGEPR IQQEEGQNQS FSNGLACLDM VLRIADVKEE DLLLQYDCLA LNLHGLRRHT VRLSRKHHHH HH
categoryamino acid composition(%)
HydrophobicI(4.8) V(5.8) L(8.3) M(1.0) A(7.1) G(6.1) P(3.8)
AromaticF(4.5) W(1.6) Y(4.5)
HydrophilicR(4.8) K(6.1) E(5.1) D(4.8) Q(5.4) N(6.4) H(3.2) S(7.1) T(6.4) C(3.2)

Abbreviated name: IL33

Annotation: Interleukin (IL)-33. Belongs to IL-1 family

GSSITGISPI TEYLASLSTY NDQSITFALE DESYEIYVED LKKDEKKDKV LLSYYESQHP SNESGDGVDG KMLMVTLSPT KDFWLHANNK EHSVELHKCE KPLPDQAFFV LHNMHSNCVS FECKTDPGVF IGVKDNHLAL IKVDSSENLC TENILFKLSE T
categoryamino acid composition(%)
HydrophobicI(5.0) V(6.2) L(10.6) M(1.9) A(3.1) G(4.3) P(3.7)
AromaticF(4.3) W(0.6) Y(3.7)
HydrophilicR(0.0) K(8.7) E(9.3) D(7.5) Q(1.9) N(5.6) H(4.3) S(11.2) T(5.6) C(2.5)