1iqa
From Proteopedia
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| - | [[Image:1iqa.jpg|left|200px]] | + | [[Image:1iqa.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MOUSE RANK LIGAND''' | + | {{Structure |
| + | |PDB= 1iqa |SIZE=350|CAPTION= <scene name='initialview01'>1iqa</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MOUSE RANK LIGAND''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IQA is a [ | + | 1IQA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQA OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11733492 11733492] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tnf]] | [[Category: tnf]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:53:27 2008'' |
Revision as of 09:53, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF MOUSE RANK LIGAND
Overview
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 Structure
1IQA is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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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