1IQA

CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MOUSE RANK LIGAND

Summary for 1IQA

• Entry DOI: 10.2210/pdb1iqa/pdb
• Descriptor: RECEPTOR ACTIVATOR OF NUCLEAR FACTOR KAPPA B LIGAND (2 entities in total)
• Functional Keywords: homotrimer, beta-strand jellyroll, rankl, rank ligand, rank, cytokine, tnf, bone remodeling, osteoclast differentiation factor
• Biological source: Mus musculus (house mouse)
• Cellular location: Isoform 1: Cell membrane; Single-pass type II membrane protein. Isoform 2: Cell membrane; Single-pass type II membrane protein. Isoform 3: Cytoplasm. Tumor necrosis factor ligand superfamily member 11, soluble form: Secreted: O35235
• Total number of polymer chains: 3
• Total formula weight: 54002.06

Authors

Ito, S.,Wakabayashi, K.,Ubukata, O.,Hayashi, S.,Okada, F.,Hata, T. (deposition date: 2001-07-11, release date: 2002-03-13, Last modification date: 2024-10-16)

Primary citation

Ito, S.,Wakabayashi, K.,Ubukata, O.,Hayashi, S.,Okada, F.,Hata, T.
Crystal structure of the extracellular domain of mouse RANK ligand at 2.2-A resolution.
J.Biol.Chem., 277:6631-6636, 2002

PubMed Abstract: Bone remodeling involves the resorption of bone by osteoclasts and the synthesis of bone matrix by osteoblasts. Receptor activator of NF-kappa B ligand (RANKL, also known as ODF and OPGL), a member of the tumor necrosis factor (TNF) family, triggers osteoclastogenesis by forming a complex with its receptor, RANK. We have determined the crystal structure of the extracellular domain of mouse RANKL at 2.2-A resolution. The structure reveals that the RANKL extracellular domain is trimeric, which was also shown by analytical ultracentrifugation, and each subunit has a beta-strand jellyroll topology like the other members of the TNF family. A comparison of RANKL with TNF beta and TNF-related apoptosis-inducing ligand (TRAIL), whose structures were determined to be in the complex form with their respective receptor, reveals conserved and specific features of RANKL in the TNF superfamily and suggests the presence of key residues of RANKL for receptor binding.

PubMed: 11733492
DOI: 10.1074/jbc.M106525200

Experimental method

X-RAY DIFFRACTION (2.2 Å)