1jh5
From Proteopedia
(New page: 200px<br /> <applet load="1jh5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jh5, resolution 3.00Å" /> '''Crystal Structure o...) |
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- | [[Image:1jh5.gif|left|200px]]<br /> | + | [[Image:1jh5.gif|left|200px]]<br /><applet load="1jh5" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1jh5" size=" | + | |
caption="1jh5, resolution 3.00Å" /> | caption="1jh5, resolution 3.00Å" /> | ||
'''Crystal Structure of sTALL-1 of TNF family ligand'''<br /> | '''Crystal Structure of sTALL-1 of TNF family ligand'''<br /> | ||
==Overview== | ==Overview== | ||
- | TALL-1/BAFF/BLyS was recently identified as a member of the tumor necrosis | + | TALL-1/BAFF/BLyS was recently identified as a member of the tumor necrosis factor (TNF) ligand family. The crystal structure of the functional soluble TALL-1 (sTALL-1) has been determined at 3.0 A. sTALL-1 forms a virus-like assembly with 200 A diameter in the crystals, containing 60 sTALL-1 monomers. The cluster formation is mediated by a "flap" region of the sTALL-1 monomer. The virus-like assembly was also detected in solution using gel filtration and electron microscopy. Deletion of the flap region disrupted the formation of the virus-like assembly. The mutant sTALL-1 still bound its receptor but could not activate NF-kappaB and did not stimulate B lymphocyte proliferation. Finally, we found the virus-like cluster of sTALL-1 exists in physiological condition. We propose that this virus-like assembly of sTALL-1 is the functional unit for TALL-1 in vivo. |
==About this Structure== | ==About this Structure== | ||
- | 1JH5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1JH5 is a [http://en.wikipedia.org/wiki/Single_protein 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=1JH5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
[[Category: Opalka, N.]] | [[Category: Opalka, N.]] | ||
- | [[Category: Shu, H | + | [[Category: Shu, H B.]] |
[[Category: Xu, L.]] | [[Category: Xu, L.]] | ||
[[Category: Zhang, G.]] | [[Category: Zhang, G.]] | ||
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[[Category: thank]] | [[Category: thank]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:33 2008'' |
Revision as of 11:22, 21 February 2008
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Crystal Structure of sTALL-1 of TNF family ligand
Overview
TALL-1/BAFF/BLyS was recently identified as a member of the tumor necrosis factor (TNF) ligand family. The crystal structure of the functional soluble TALL-1 (sTALL-1) has been determined at 3.0 A. sTALL-1 forms a virus-like assembly with 200 A diameter in the crystals, containing 60 sTALL-1 monomers. The cluster formation is mediated by a "flap" region of the sTALL-1 monomer. The virus-like assembly was also detected in solution using gel filtration and electron microscopy. Deletion of the flap region disrupted the formation of the virus-like assembly. The mutant sTALL-1 still bound its receptor but could not activate NF-kappaB and did not stimulate B lymphocyte proliferation. Finally, we found the virus-like cluster of sTALL-1 exists in physiological condition. We propose that this virus-like assembly of sTALL-1 is the functional unit for TALL-1 in vivo.
About this Structure
1JH5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands., Liu Y, Xu L, Opalka N, Kappler J, Shu HB, Zhang G, Cell. 2002 Feb 8;108(3):383-94. PMID:11853672
Page seeded by OCA on Thu Feb 21 13:22:33 2008
Categories: Homo sapiens | Single protein | Liu, Y. | Opalka, N. | Shu, H B. | Xu, L. | Zhang, G. | Baff | Blys | Tall-1 | Thank