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1L0A

DOWNSTREAM REGULATOR TANK BINDS TO THE CD40 RECOGNITION SITE ON TRAF3

Summary for 1L0A
Entry DOI10.2210/pdb1l0a/pdb
Related1KZZ
DescriptorTNF receptor associated factor 3, TRAF family member-associated NF-kappa-b activator (3 entities in total)
Functional Keywordscd40, nf-kb signaling, tank, tnf receptor, traf3, signaling protein
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm : Q13114 Q92844
Total number of polymer chains2
Total formula weight23887.48
Authors
Li, C.,Ni, C.-Z.,Havert, M.L.,Cabezas, E.,He, J.,Kaiser, D.,Reed, J.C.,Satterthwait, A.C.,Cheng, G.,Ely, K.R. (deposition date: 2002-02-08, release date: 2002-04-10, Last modification date: 2024-02-14)
Primary citationLi, C.,Ni, C.Z.,Havert, M.L.,Cabezas, E.,He, J.,Kaiser, D.,Reed, J.C.,Satterthwait, A.C.,Cheng, G.,Ely, K.R.
Downstream regulator TANK binds to the CD40 recognition site on TRAF3.
Structure, 10:403-411, 2002
Cited by
PubMed Abstract: TRAFs (tumor necrosis factor receptor [TNFR]-associated factors) bind to the cytoplasmic portion of liganded TNFRs and stimulate activation of NF-kappaB or JNK pathways. A modulator of TRAF signaling, TANK, serves as either an enhancer or an inhibitor of TRAF-mediated signaling pathways. The crystal structure of a region of TANK bound to TRAF3 has been determined and compared to a similar CD40/TRAF3 complex. TANK and CD40 bind to the same crevice on TRAF3. The recognition motif PxQxT is presented in a boomerang-like structure in TANK that is markedly different from the hairpin loop that forms in CD40 upon binding to TRAF3. Critical TANK contact residues were confirmed by mutagenesis to be required for binding to TRAF3 or TRAF2. Binding affinity, measured by isothermal titration calorimetry and competition assays, demonstrated that TANK competes with CD40 for the TRAF binding site.
PubMed: 12005438
DOI: 10.1016/S0969-2126(02)00733-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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