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1otz
From Proteopedia
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| - | [[Image:1otz.gif|left|200px]] | + | [[Image:1otz.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the BAFF-BAFF-R complex (part I)''' | + | {{Structure |
| + | |PDB= 1otz |SIZE=350|CAPTION= <scene name='initialview01'>1otz</scene>, resolution 3.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the BAFF-BAFF-R complex (part I)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OTZ is a [ | + | 1OTZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTZ OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation., Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO, Nat Struct Biol. 2003 May;10(5):342-8. PMID:[http:// | + | Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation., Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO, Nat Struct Biol. 2003 May;10(5):342-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12715002 12715002] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''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 13:15:37 2008'' |
Revision as of 11:15, 20 March 2008
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| , resolution 3.3Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the BAFF-BAFF-R complex (part I)
Overview
B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACI and BAFF-R. We have determined the crystal structure of the extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 A. The cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the beta-turn and is indispensable in the binding of BAFF. The crystal structure shows that a unique dimeric contact occurs between the BAFF-R monomers in the virus-like cage complex. The extracellular domain of TACI contains two CRDs, both of which contain the DxL motif. Modeling of TACI-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage.
About this Structure
1OTZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation., Kim HM, Yu KS, Lee ME, Shin DR, Kim YS, Paik SG, Yoo OJ, Lee H, Lee JO, Nat Struct Biol. 2003 May;10(5):342-8. PMID:12715002
Page seeded by OCA on Thu Mar 20 13:15:37 2008
