1L0A
DOWNSTREAM REGULATOR TANK BINDS TO THE CD40 RECOGNITION SITE ON TRAF3
Summary for 1L0A
Entry DOI | 10.2210/pdb1l0a/pdb |
Related | 1KZZ |
Descriptor | TNF receptor associated factor 3, TRAF family member-associated NF-kappa-b activator (3 entities in total) |
Functional Keywords | cd40, nf-kb signaling, tank, tnf receptor, traf3, signaling protein |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm : Q13114 Q92844 |
Total number of polymer chains | 2 |
Total formula weight | 23887.48 |
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 citation | 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. 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: 12005438DOI: 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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