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Volume 10, Issue 8 (Suppl) J Proteomics Bioinform, an open access journal
ISSN: 0974-276X Structural Biology 2017
September 18-20, 2017
9th International Conference on
Structural Biology
September 18-20, 2017 Zurich, Switzerland
Shin-ichi Tate, J Proteomics Bioinform 2017, 10:8(Suppl)
DOI: 10.4172/0974-276X-C1-0100
Inter-domain communication through intrinsically disordered region (IDR) revealed through the
ensemble structure analysis
Shin-ichi Tate
Hiroshima University, Japan
The functionally relevant inter-domain communication between the domains linked by intrinsically disordered region was
explored by NMR in combination with small angle X-ray scattering. Based on the ensemble structure analyses and the
numerical simulations to reproduce the chemical shift changes along with the substrate concentration, we have demonstrated
how the domains cooperate to enhance the protein function through the substantially dynamic spatial allocation of the domains.
Pin1, a proline cis/trans isomerase, comprises two domains linked by 10-residue IDR, one is the substrate biding domain to
recognize pSer/pThr-Pro motif and the other is the enzyme domain that rotates the Pro peptide bond in the motif. The enzyme
domain shows very limited affinity to the substrate, but its binding ability was enhanced by two orders of magnitude in the
presence of the substrate binding domain linked by IDR; in which the inter-domain fly-casting mechanism plays to keep the
substrate bound to Pin1 by tossing and receiving the substrate between the domains, once the substrate in bound to either one
of the domains. A new functional aspect of IDR will be addressed.
Biography
Shin-ichi Tate has got his PhD degree from the University of Tokyo in 1993. He has the experience as a visiting Researcher at ETH (Prof. K Wühtrich) and NIH (Dr.
A Bax). He has been a Professor in the Department of Mathematical and Life Sciences at Hiroshima since 2006. He is now the Director of the Research Center for
the Mathematics on Chromatin live Dynamics (RcMcd), and the Dean of the School of Science in Hiroshima University.
Figure1: Inter-domain substrate migration mechanism
to enhance the binding ability of the enzyme domain by
200-fold. In this process, the IDR roles in prompting the
domains to efficiently capture the substrate by allowing
them for searching the substrate in a wide space, as
analogously described as fly-casting.