2jmd
From Proteopedia
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Solution Structure of the Ring Domain of Human TRAF6
Overview
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.
About this Structure
2JMD is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure, interactions, and dynamics of the RING domain from human TRAF6., Mercier P, Lewis MJ, Hau DD, Saltibus LF, Xiao W, Spyracopoulos L, Protein Sci. 2007 Apr;16(4):602-14. Epub 2007 Feb 27. PMID:17327397
Page seeded by OCA on Mon Nov 12 22:56:27 2007
