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Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded
by the complexity of producing the receptor protein. In this study, the researchers from Australia, USA, United Kingdom and Czech Republic present the
first view of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin or highly
potent insulin analogue developed in IOCB in Prague (Dr. Jiří Jiráček group) bound to truncated insulin receptor constructs. Together, our findings provide an explanation for a wealth
of biochemical data from the insulin receptor and IGF-1 receptor systems relevant to the design of therapeutic insulin analogues.
John G. Menting, Jonathan Whittaker, Mai B. Margetts, Linda J. Whittaker, Geoffrey K. W. Kong, Brian J. Smith, Christopher J. Watson, Lenka Žáková, Emília Kletvíková, Jiří Jiráček,
Shu Jin Chan, Donald F. Steiner, Guy G. Dodson, Andrzej M. Brzozowski, Michael A. Weiss, Colin W. Ward & Michael C. Lawrence.:
How insulin engages its primary binding site on the insulin receptor.
Nature 493, 241-245 (2013).
Gongrats !
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