Abstract
AbstractA three‐dimensional model of interleukin‐4 (IL‐4) bound to one molecule each of the high‐ and low‐affinity receptors (IL‐4R and IL‐2Rγ) was built, using the crystal structure of the complex of human growth hormone (HGH) with its receptor (HGHR) as a starting model. The modeling of IL‐4 with its receptors was based on the conservation of the sequences and on the predicted structural organization for cytokine receptors, and assuming that the binding mode of the ligands would be similar. Analysis of the interface between IL‐4 and both receptor molecules was carried out to reveal which residues are important for complex formation. The modeling procedures showed that there were no major problems in maintaining a reasonable fit of IL‐4 with the two receptor molecules, in a manner analogous to the complex of HGH–HGHR. Many of the residues that appear by modeling to be important for binding between IL‐4 and the receptors have been previously implicated in that role by different methods. A striking motif of aromatic and positively charged residues on the surface of the C‐terminal domains of the receptors is highly conserved in the structure of HGH–HGHR and in the models of IL‐4 complexed with its receptors. © 1995 Wiley‐Liss, Inc.
References
53
Referenced
23
10.1016/0959-440X(93)90144-A
10.1126/science.1549776
10.1016/0022-2836(92)90457-U
10.1016/0014-5793(92)80739-4
10.1016/S0021-9258(19)88711-2
10.1126/science.256.5064.1673
10.1126/science.257.5068.412
10.1126/science.1837174
10.1016/0022-2836(92)90470-5
10.1002/j.1460-2075.1992.tb05396.x
10.1126/science.1455231
10.1038/363172a0
10.1073/pnas.90.11.5167
10.1016/S0021-9258(18)54706-2
/ J. Biol. Chem. / Crystal structure of recombinant rabbit interferon‐γ at 2.7‐Å resolution by Samudzi C. T. (1991)10.1126/science.1902591
10.1073/pnas.87.18.6934
10.1016/S0969-2126(00)00018-6
10.1016/S0969-2126(00)00034-4
{'key': 'e_1_2_1_20_2', 'first-page': '3111', 'article-title': 'The human growth hormone receptor', 'volume': '265', 'author': 'Fuh G.', 'year': '1990', 'journal-title': 'J. Biol. Chem.'}
/ J. Biol. Chem. / The human growth hormone receptor by Fuh G. (1990)10.1016/0092-8674(89)90295-X
- Neidhart L. R. Favara J. P. Lie W‐R. Leimgruber R. M. Levine A. D.Purification and characterization of recombinant soluble human interleukin 4 receptor.J. Biol. Chem. in press 1994.
10.1016/S0021-9258(19)36712-2
/ J. Biol. Chem. / The interleukin‐4 related lymphokines and their binding to hematopoietin receptors by Boulay J‐L. (1992)10.1002/prot.340170105
10.1002/pro.5560020902
10.1126/science.8266076
10.1126/science.8266078
-
Leonard W. J.The defective gene in X‐linked severe combined immunodeficiency encodes a shared interleukin receptor subunit: implications for cytokine pleiotropy and redundancy.Current Opinion Immunol. in press 1994.
(
10.1016/0952-7915(94)90152-X
) 10.1016/0014-5793(94)00496-X
10.1126/science.1631559
10.1016/0076-6879(85)15014-7
{'key': 'e_1_2_1_32_2', 'volume-title': 'X‐PLOR: A System for X‐Ray Crystallography and NMR', 'author': 'Brunger A.', 'year': '1992'}
/ X‐PLOR: A System for X‐Ray Crystallography and NMR by Brunger A. (1992)10.1007/BF01593790
10.1126/science.1279805
10.1016/0896-6273(94)90326-3
10.1038/348411a0
10.1038/348419a0
10.1016/0022-2836(87)90412-8
10.1038/342877a0
10.1038/342248a0
10.1002/j.1460-2075.1993.tb06207.x
10.1111/j.1432-1033.1994.tb18890.x
10.1002/j.1460-2075.1992.tb05401.x
10.1016/S0021-9258(18)48382-2
/ J. Biol. Chem. / Structure of mouse interleukin 3 (IL‐3) binding protein (AIC2A) by Wang H.‐M. (1992)10.1016/S0021-9258(18)42192-8
/ J. Biol. Chem. / Receptor binding and internalization of mouse interleukin‐2 derivatives that are partial agonists by Imler J.‐L. (1992)10.1084/jem.171.3.861
10.1016/0092-8674(90)90208-V
10.1016/0968-0004(90)90051-C
10.1126/science.2404337
10.1016/0092-8674(90)90342-C
10.1002/j.1460-2075.1991.tb04881.x
10.1016/S0021-9258(19)49956-0
/ J. Biol. Chem. / Mutations in the trp‐ser‐x‐try‐ser motif of the erythropoeitin receptor abolish processing, ligand binding, and activation of the receptor by Yoshimura A. (1992)10.1128/MCB.12.1.240
10.1016/S0021-9258(18)38125-0
/ J. Biol. Chem. / Predominant contribution of surface approximation to the mechanism of heparin acceleration, the antithrombin‐thrombin reaction by Olson S. T. (1991)
Dates
Type | When |
---|---|
Created | 20 years, 3 months ago (May 28, 2005, 9:39 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 25, 2023, 2:18 p.m.) |
Indexed | 1 year, 7 months ago (Jan. 13, 2024, 12:27 a.m.) |
Issued | 30 years, 6 months ago (Feb. 1, 1995) |
Published | 30 years, 6 months ago (Feb. 1, 1995) |
Published Online | 21 years, 6 months ago (Feb. 3, 2004) |
Published Print | 30 years, 6 months ago (Feb. 1, 1995) |
@article{Gustchina_1995, title={A model of the complex between interleukin‐4 and its receptors}, volume={21}, ISSN={1097-0134}, url={http://dx.doi.org/10.1002/prot.340210208}, DOI={10.1002/prot.340210208}, number={2}, journal={Proteins: Structure, Function, and Bioinformatics}, publisher={Wiley}, author={Gustchina, Alla and Zdanov, Alexander and Schalk‐Hihi, Céline and Wlodawer, Alexander}, year={1995}, month=feb, pages={140–148} }