First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
|theoretically, and hence should be interpreted with caution.|
THEORETICAL STRUCTURE OF HUMAN INTERLEUKIN-13
Interleukin-13 (IL-13) plays a key role in immune responses and inflammation. A structural model of human IL-13 (HuIL-13) based on the nuclear magnetic resonance and X-ray structure of IL-4 is put forward. Unlike previous models, this model is based on new sequence alignments that take into account the formation of the two disulfide linkages that have been determined experimentally. The proposed structure of human IL-13 is similar to IL-4, consisting of a four helix bundle with hydrophobic residues lining the core of the molecule and surface polar residues showing a high degree of solvent accessibility. Regions of HuIL-13 that are critical for the interaction with its receptors are explored and discussed in relation to existing mutagenic studies. From these studies we predict that helices A and C of HuIL-13 interact with the IL-4 receptor alpha (IL-4Ralpha) region and helix D is responsible for the interaction with the IL-13 receptor alpha 1 (IL-13Ralpha1) receptor.
Structural model of human IL-13 defines the spatial interactions with the IL-13Ralpha/IL-4Ralpha receptor., Zuegg J, Webb DC, Foster PS, Casarotto MG, Immunol Cell Biol. 2001 Aug;79(4):332-9. PMID:11488979
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.