The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction.
High-affinity, high-selectivity protein-protein interactions that are critical for cell survival present an evolutionary paradox: How does selectivity evolve when acquired mutations risk a lethal loss of high-affinity binding? A detailed understanding of selectivity in such complexes requires struct...
Prif Awduron: | Meenan, N, Sharma, A, Fleishman, S, Macdonald, C, Morel, B, Boetzel, R, Moore, G, Baker, D, Kleanthous, K |
---|---|
Fformat: | Journal article |
Iaith: | English |
Cyhoeddwyd: |
2010
|
Eitemau Tebyg
-
Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.
gan: Keeble, A, et al.
Cyhoeddwyd: (2008) -
Following evolutionary paths to protein-protein interactions with high affinity and selectivity.
gan: Levin, K, et al.
Cyhoeddwyd: (2009) -
Structure of the ultra-high-affinity colicin E2 DNase--Im2 complex.
gan: Wojdyla, J, et al.
Cyhoeddwyd: (2012) -
Structure of the ultra-high-affinity colicin E2 DNase-Im2 complex
gan: Wojdyla, J, et al.
Cyhoeddwyd: (2012) -
Consequences of inducing intrinsic disorder in a high-affinity protein-protein interaction.
gan: Papadakos, G, et al.
Cyhoeddwyd: (2015)