Journal article

SPRY Domain-Containing SOCS Box Protein 2: Crystal Structure and Residues Critical for Protein Binding

Z Kuang, S Yao, Y Xu, RS Lewis, A Low, SL Masters, TA Willson, TB Kolesnik, SE Nicholson, TJP Garrett, RS Norton

Journal of Molecular Biology | Elsevier | Published : 2009


The four mammalian SPRY (a sequence repeat in dual-specificity kinase splA and ryanodine receptors) domain-containing suppressor of cytokine signalling (SOCS) box proteins (SSB-1 to -4) are characterised by a C-terminal SOCS box and a central SPRY domain. The latter is a protein interaction module found in over 1600 proteins, with more than 70 encoded in the human genome. Here we report the crystal structure of the SPRY domain of murine SSB-2 and compare it with the SSB-2 solution structure and crystal structures of other B30.2/SPRY domain-containing family proteins. The structure is a bent β-sandwich, consisting of two seven-stranded β-sheets wrapped around a long loop that extends from the..

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Awarded by National Health and Medical Research Council, Australia


Funding Acknowledgements

This work was supported in part by the National Health and Medical Research Council, Australia (program grant 461219 and project grant 461233 to R.S.N. and S.E.N., program grant 280912 to T.P.J.G., fellowships to R.S.N., S.E.N. and TP.J.G., and an NHMRC IRIISS grant 361646), as well as a Victorian State Government OIS grant. We thank Dr Janet Newman at the Bio21 collaborative crystallization centre (0) for assistance and valuable discussions, Dr Jian-Guo Zhang for assistance with protein purification, and Mr Oliver Clarke for assistance.