1IJZ
Solution Structure of Human IL-13
Summary for 1IJZ
Entry DOI | 10.2210/pdb1ijz/pdb |
Related | 1IK0 |
Descriptor | INTERLEUKIN-13 (1 entity in total) |
Functional Keywords | left-handed four-helix bundle, cytokine |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P35225 |
Total number of polymer chains | 1 |
Total formula weight | 12490.58 |
Authors | Moy, F.J.,Diblasio, E.,Wilhelm, J.,Powers, R. (deposition date: 2001-05-01, release date: 2002-05-01, Last modification date: 2024-10-30) |
Primary citation | Moy, F.J.,Diblasio, E.,Wilhelm, J.,Powers, R. Solution structure of human IL-13 and implication for receptor binding. J.Mol.Biol., 310:219-230, 2001 Cited by PubMed Abstract: Interleukin-13 has been implicated as a key factor in asthma, allergy, atopy and inflammatory response, establishing the protein as a valuable therapeutic target. The high-resolution solution structure of human IL-13 has been determined by multidimensional NMR. The resulting structure is consistent with previous short-chain left-handed four-helix bundles, where a significant similarity in the folding topology between IL-13 and IL-4 was observed. IL-13 shares a significant overlap in biological function with IL-4, a result of the common alpha chain component (IL-4Ralpha) in their respective receptors. Based on the available structural and mutational data, an IL-13/IL-4Ralpha model and a sequential mechanism for forming the signaling heterodimer is proposed for IL-13. PubMed: 11419948DOI: 10.1006/jmbi.2001.4764 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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