4kgg
From Proteopedia
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[[Category: Bonanno, J B.]] | [[Category: Bonanno, J B.]] | ||
[[Category: IFN, Atoms-to-Animals:.The Immune Function Network.]] | [[Category: IFN, Atoms-to-Animals:.The Immune Function Network.]] | ||
| + | [[Category: Kumar, P R.]] | ||
[[Category: Liu, W.]] | [[Category: Liu, W.]] | ||
[[Category: NYSGRC, New York Structural Genomics Research Consortium.]] | [[Category: NYSGRC, New York Structural Genomics Research Consortium.]] | ||
[[Category: Nathenson, S G.]] | [[Category: Nathenson, S G.]] | ||
| - | [[Category: Prakash, R.]] | ||
[[Category: Toro, R.]] | [[Category: Toro, R.]] | ||
[[Category: Zhan, C.]] | [[Category: Zhan, C.]] | ||
Revision as of 02:34, 20 September 2013
Contents |
Crystal structure of light mutant2 and dcr3 complex
Function
[TNF6B_HUMAN] Decoy receptor that can neutralize the cytotoxic ligands TNFS14/LIGHT, TNFSF15 and TNFSF6/FASL. Protects against apoptosis.[1] [TNF14_HUMAN] Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Activates NFKB, stimulates the proliferation of T-cells, and inhibits growth of the adenocarcinoma HT-29. Acts as a receptor for Herpes simplex virus.
About this Structure
4kgg is a 4 chain structure with sequence from Clostridium acetobutylicum and Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ Zhan C, Patskovsky Y, Yan Q, Li Z, Ramagopal U, Cheng H, Brenowitz M, Hui X, Nathenson SG, Almo SC. Decoy Strategies: The Structure of TL1A:DcR3 Complex. Structure. 2011 Feb 9;19(2):162-71. PMID:21300286 doi:10.1016/j.str.2010.12.004
Categories: Clostridium acetobutylicum | Homo sapiens | Almo, S C. | Bonanno, J B. | IFN, Atoms-to-Animals:.The Immune Function Network. | Kumar, P R. | Liu, W. | NYSGRC, New York Structural Genomics Research Consortium. | Nathenson, S G. | Toro, R. | Zhan, C. | Atoms-to-animals: the immune function network | Bind tnf receptor hvem and ltbr | Cytokine | Cytokine-signaling protein complex | Dcr3 | Ifn | Immune system | Jelly-roll fold | Light | Ltbr | Membrane | N-glycosylation | New hvem | New york structural genomics research consortium | Nysgrc | Protein structure initiative | Psi-biology | Secreted protein | Structural genomic | Tnf | Tnf14 | Tnfr
