Abstract
The S100B protein is an intra- and extracellular signaling protein that plays a role in a multitude of cellular processes and abnormal S100B is associated with various neurological diseases and cancers. S100B recognizes and binds effector proteins in a calcium-dependent manner. S100B has been shown to interact with the actin capping protein CapZ, protein kinase C, Hdm2 and 4, RAGE receptor, and p53, among others. These protein partners interact with a common area on the S100B protein surface, validating the method of using the consensus sequence for S100B target search. In addition, each S100B target protein distinguishes itself by additional contacts with S100B. This perspective suggests that the combination of sequence homology search and structural analysis promises to identify newer S100B-binding partners beyond the use of the consensus sequence alone as the given example in the XPB subunit of the TFIIH general transcription factor. XPB is a helicase required for both transcription and DNA repair. Inherited xpb mutations are associated with human disease Xeroderma Pigmentasum, Cockayne syndrome, and trichothiodystrophy. S100B protein is likely associated with much more biological pathways and processes. We believe that S100B will attract more and more attentions in the scientific community and S100B related studies will have important implications in human health and medicine.
Highlights
The S100B protein belongs to the S100 family of Ca2+-binding signaling proteins which share dual conserved calcium-binding EF- hand motifs
We identified a new potential target of S100B in the Xeroderma pigmentosum complementation group B (XPB) helicase subunit of the general transcription factor TFIIH
We notice that the XPB extreme C-terminus shares sequence homology with key residues of the p53-carboxy-terminal regulatory domain (CTD), and so we propose that XPB should interact with S100B in a similar fashion to that of the p53-S100B complex [44]
Summary
The S100B protein belongs to the S100 family of Ca2+-binding signaling proteins which share dual conserved calcium-binding EF- hand motifs. S100B has been reported to interact with a variety of protein targets including the p53 tumor suppressor, CapZ, the RAGE receptor, NDR kinase, neurotensin, cathepsin L inhibitor, Hdm, Hdm, protein kinase Cα, ROS-GC1, microtubule-associated tau proteins, melittin, amyloid-β, interleukin-11, the serotonin 5-HT7 receptor, the dopamine D2 receptor and RSK1 [15,16,17,18,19,20,21,22,23,24,25,26,27,28,29]. This short perspective focuses on the structural basis of S100B-protein interactions
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