11 research outputs found
Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site.
The structure of a folded core of IL-16 is similar to that of intracellular protein modules called PDZ domains. IL-16 is thus the first extracellular protein found to have a PDZ-like fold. However, it does not exhibit normal peptide binding properties of PDZ domains. This is due to alterations of the structure at the 'PDZ-like binding site' of IL-16 (the GLGF cleft): the GLGF cleft of IL-16 is much smaller than those of PDZ-domains and is additionally blocked with a tryptophan side chain at its center. Our experiments indicate also that IL-16 nonspecifically aggregates in solution; but formation of a homo-tetrameric protein is not required, in contrast to previous suggestions, for its chemo-attractant activity
Contextualising Apartheid at the End of Empire: Repression, ‘Development’ and the Bantustans
This article examines the global dynamics of late colonialism and how these informed
South African apartheid. More specifically, it locates the programmes of mass
relocation and bantustan ‘self-government’ that characterised apartheid after 1959 in
relation to three key dimensions. Firstly, the article explores the global circulation of
idioms of ‘development’ and trusteeship in the first half of the twentieth century and its
significance in shaping segregationist policy; secondly, it situates bantustan ‘selfgovernment’
in relation to the history of decolonisation and the partitions and
federations that emerged as late colonial solutions; and, thirdly, it locates the
tightening of rural village planning in the bantustans after 1960 in relation to the
elaboration of anti-colonial liberation struggles, repressive southern African settler
politics and the Cold War. It argues that, far from developing policies that were at odds
with the global ‘wind of change’, South African apartheid during the 1960s and 1970s
reflected much that was characteristic about late colonial strategy