2YOP

Long wavelength S-SAD structure of FAM3B PANDER

Summary for 2YOP

• Entry DOI: 10.2210/pdb2yop/pdb
• Related: 2YOQ
• Descriptor: PROTEIN FAM3B, GLYCEROL (3 entities in total)
• Functional Keywords: apoptosis, fam3, diabetes, ilei, emt
• Biological source: MUS MUSCULUS (MOUSE)
• Cellular location: Secreted (By similarity): Q9D309
• Total number of polymer chains: 3
• Total formula weight: 66759.72

Authors

Johansson, P.,Bernstrom, J.,Gorman, T.,Oster, L.,Backstrom, S.,Schweikart, F.,Xu, B.,Xue, Y.,Holmberg Schiavone, L. (deposition date: 2012-10-26, release date: 2013-01-30, Last modification date: 2024-11-20)

Primary citation

Johansson, P.,Bernstrom, J.,Gorman, T.,Oster, L.,Backstrom, S.,Schweikart, F.,Xu, B.,Xue, Y.,Schiavone, L.H.
Fam3B Pander and Fam3C Ilei Represent a Distinct Class of Signaling Molecules with a Non-Cytokine-Like Fold.
Structure, 21:306-, 2013

PubMed Abstract: The FAM3 superfamily is predicted to contain classical four-helix bundle cytokines, featuring a typical up-up-down-down fold. Two members of FAM3 have been extensively studied. FAM3B PANDER has been shown to regulate glucose homeostasis and β cell function, whereas the homologous FAM3C ILEI has been shown to be involved in epithelial-mesenchymal transition and cancer. Here, we present a three-dimensional structure of a FAM3 protein, murine PANDER. Contrary to previous suggestions, PANDER exhibits a globular β-β-α fold. The structure is composed of two antiparallel β sheets lined by three short helices packing to form a highly conserved water-filled cavity. The fold shares no relation to the predicted four-helix cytokines but is conserved throughout the FAM3 superfamily. The available biological data and the unexpected new fold indicate that FAM3 PANDER and ILEI could represent a new structural class of signaling molecules, with a different mode of action compared to the traditional four-helix bundle cytokines.

PubMed: 23333428
DOI: 10.1016/J.STR.2012.12.009

Experimental method

X-RAY DIFFRACTION (2.3 Å)