1iqa
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CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MOUSE RANK LIGAND
OverviewOverview
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.
About this StructureAbout this Structure
1IQA is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the extracellular domain of mouse RANK ligand at 2.2-A resolution., Ito S, Wakabayashi K, Ubukata O, Hayashi S, Okada F, Hata T, J Biol Chem. 2002 Feb 22;277(8):6631-6. Epub 2001 Nov 30. PMID:11733492
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