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. Author manuscript; available in PMC: 2015 May 3.
Published in final edited form as: Biochemistry. 2013 Dec 10;52(51):9141–9154. doi: 10.1021/bi401368r

Figure 4.

Figure 4

Role of individual cysteine residues in NEMO dimerization and aggregation. (A) Panel of 6xAla NEMO mutants in which each of the cysteines in the region of NEMO sequence between residue 1 and 395 has been individually added back into the 7xAla construct. (B) SDS-PAGE analysis of the 6xAla mutant panel under reducing (left) and non-reducing (right) conditions, showing that the mutants containing cysteines at positions 11, 54, 76 and 347 show a propensity to form disulfide-linked covalent dimers. (C) Images of the published co-crystal structure of NEMO(44-111) with IKKβ(701-745) (30), showing that the cysteines at position 54 (left) are well-positioned to form an inter-chain disulfide bond in the active conformation of the protein, while the cysteines at position 76 are not as their sulfur atoms are separated by 12.7 Å.