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. 2011 Jun;50(2):103-17.
doi: 10.1007/s10858-011-9505-5. Epub 2011 Apr 26.

Solution Structure, Dynamics and Thermodynamics of the Three SH3 Domains of CD2AP

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Solution Structure, Dynamics and Thermodynamics of the Three SH3 Domains of CD2AP

Jose L Ortega Roldan et al. J Biomol NMR. .

Abstract

CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin. To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability and the backbone dynamics have been related to the structural features of each domain using the structure-based FoldX algorithm. We have found that the N-terminal SH3 domain of both adaptor proteins CD2AP and CIN85 are the most stable SH3 domains that have been studied until now. This high stability is driven by a more extensive network of intra-molecular interactions. We believe that this increased stabilization of N-terminal SH3 domains in adaptor proteins is crucial to maintain the necessary conformation to establish the proper interactions critical for the recruitment of their natural targets.

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References

    1. J Mol Biol. 2001 Nov 2;313(4):873-87 - PubMed
    1. Methods Enzymol. 1998;295:100-27 - PubMed
    1. J Mol Biol. 1998 Feb 27;276(3):657-67 - PubMed
    1. Biochemistry. 1996 Feb 13;35(6):1722-32 - PubMed
    1. Biochemistry. 2008 May 27;47(21):5795-803 - PubMed

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