2JMD

Solution Structure of the Ring Domain of Human TRAF6

Summary for 2JMD

• Entry DOI: 10.2210/pdb2jmd/pdb
• Related: 1CHC 1E4U 1JM7 1LB4
• Descriptor: TNF receptor-associated factor 6, ZINC ION (2 entities in total)
• Functional Keywords: protein, zinc-binding, human tnf receptor-associated factor 6, zn2+ coordination, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9Y4K3
• Total number of polymer chains: 1
• Total formula weight: 7145.07

Authors

Mercier, P.,Lewis, M.J.,Hau, D.D.,Saltibus, L.F.,Xiao, W.,Spyracopoulos, L. (deposition date: 2006-11-02, release date: 2007-04-10, Last modification date: 2023-12-20)

Primary citation

Mercier, P.,Lewis, M.J.,Hau, D.D.,Saltibus, L.F.,Xiao, W.,Spyracopoulos, L.
Structure, interactions, and dynamics of the RING domain from human TRAF6
Protein Sci., 16:602-614, 2007

PubMed Abstract: A key step in the signaling cascade responsible for activation of the transcription factor NF-kappaB involves Lys63-linked polyubiquitination of TRAF6. Covalent attachment of ubiquitin (Ub) to TRAF6, and subsequent poly(Ub) chain synthesis, is catalyzed by the hUev1a-hUbc13 heterodimer. hUbc13 is a catalytically competent E2 enzyme, and hUev1a is an E2-like protein that binds substrate Ub. The hUev1a-hUbc13 heterodimer is targeted to TRAF6 through interactions between hUbc13 and the N-terminal RING domain from TRAF6. Nuclear magnetic resonance (NMR) spectroscopy was used to determine the solution state structure of the RING domain from human TRAF6, and the interaction between hUbc13 and TRAF6 was characterized using NMR chemical shift mapping. The main-chain dynamics of the RING domain from TRAF6 were studied using (15)N NMR relaxation. Analysis of the main-chain dynamics data indicates that residues within the alpha-helix and beta-sheet of the RING domain are as rigid as regions of canonical secondary structure in larger proteins, consistent with the biological role of RING-domain E3 proteins, which requires that the E3 contain a recognition site for recruitment of E2 ubiquitin conjugation enzymes.

PubMed: 17327397
DOI: 10.1110/ps.062358007

Experimental method

SOLUTION NMR