Journal:JBIC:3
From Proteopedia
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Structural characterization of human S100A16, a low-affinity calcium binder
Elena Babini • Ivano Bertini • Valentina Borsi • Vito Calderone • Xiaoyu Hu • Claudio Luchinat • Giacomo Parigi[1]
Molecular Tour
is a special member of the S100 class of proteins, because it upon calcium(II) binding. This was observed after determination of the solution structures of apo and calcium(II)-bound S100A16 and the crystal structure of apo S100A16. The likely reason for minimal conformational change < is the lower calcium binding affinity and present in this protein with respect to other S100 proteins. Another characteristic of is that the helix IV has the and because of a . Based on the available structures of S100 members, we analyzed and summarized all their conformational changes due to calcium(II) binding by a principal component analysis. was proved by both NMR titration and Isothermal Titration Calorimetry (ITC) experiments. Even if the , these experimental data indicated that S100A16 can . NMR relaxation are the most . Although the biological function of S100A16 is still unclear yet, these structural and dynamic properties can provide useful information for further functional studies.
