S100蛋白
S100蛋白（英语：S100 proteins）是一种脊椎动物的低分子量蛋白质家族，具有两个碱性螺旋-环-螺旋的钙结合位点（EF手型）。已知有21种不同的S100蛋白[1]。编码这些蛋白的基因家族的基因以S100为前缀，如S100A1, S100A2, S100A3等。 这一家族的蛋白也被视为是损伤相关分子模式（Damage-associated molecular pattern，DAMP）的分子。
| S100/ICaBP type calcium binding domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of the S100B protein. Based on PyMOL rendering of PDB 1b4c. | |||||||||||
| 鉴定 | |||||||||||
| 标志 | S_100 | ||||||||||
| Pfam | PF01023（旧版） | ||||||||||
| InterPro | IPR013787 | ||||||||||
| PROSITE | PDOC00275 | ||||||||||
| SCOP | 1cnp / SUPFAM | ||||||||||
| |||||||||||
相关的人类基因
编辑- S100A1，S100A2，S100A3，S100A4，S100A5，S100A6，S100A7（银屑病素）， S100A8，S100A9（8和9的异二聚体称为钙卫蛋白），S100A10，S100A11，S100A12（钙粒蛋白C），S100A13，S100A14，S100A15（koebnerisin），S100A16
- S100B
- S100P[2][3]
参考文献
编辑- ^ Marenholz I, Heizmann CW, Fritz G. S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature). Biochem. Biophys. Res. Commun. October 2004, 322 (4): 1111–22. PMID 15336958. doi:10.1016/j.bbrc.2004.07.096.
- ^ Penumutchu, Srinivasa R.; Chou, Ruey-Hwang; Yu, Chin. Structural Insights into Calcium-Bound S100P and the V Domain of the RAGE Complex. PLOS ONE. 2014-08-01, 9 (8): e103947 [2020-09-26]. ISSN 1932-6203. PMC 4118983
. PMID 25084534. doi:10.1371/journal.pone.0103947. （原始内容存档于2017-01-12）.
- ^ Penumutchu, Srinivasa R.; Chou, Ruey-Hwang; Yu, Chin. Interaction between S100P and the anti-allergy drug cromolyn. Biochemical and Biophysical Research Communications. 2014-10-17, 454 (3): 404–409. ISSN 1090-2104. PMID 25450399. doi:10.1016/j.bbrc.2014.10.048.
延伸阅读
编辑- Wolf R, Voscopoulos CJ, FitzGerald PC, et al. The mouse S100A15 ortholog parallels genomic organization, structure, gene expression, and protein-processing pattern of the human S100A7/A15 subfamily during epidermal maturation. J. Invest. Dermatol. 2006, 126 (7): 1600–8. PMID 16528363. doi:10.1038/sj.jid.5700210.
- Ronald Wolf, O. M. Zack Howard, Hui-Fang Dong, Christopher Voscopoulos, Karen Boeshans, Jason Winston, Rao Divi, Michele Gunsior, Paul Goldsmith, Bijan Ahvazi, Triantafyllos Chavakis, Joost J. Oppenheim and Stuart H. Yuspa. Chemotactic Activity of S100A7 (Psoriasin) Is Mediated by the Receptor for Advanced Glycation End Products and Potentiates Inflammation with Highly Homologous but Functionally Distinct S100A15.. The Journal of Immunology. 2010, 181 (2): 1499–1506.
- Ronald Wolf, Christopher Voscopoulos, Jason Winston, Alif Dharamsi, Paul Goldsmith Michele Gunsior, Barbara K. Vonderhaar, Melanie Olson, Peter H. Watson, and Stuart H. Yuspa. Highly homologous hS100A15 and hS100A7 proteins are distinctly expressed in normal breast tissue and breast cancer.. J. Cancer Lett. 2008, 277 (1): 101–107. PMC 2680177 . PMID 19136201. doi:10.1016/j.canlet.2008.11.032.
- Ronald Wolf, Francesca Mascia, Alif Dharamsi, O. M. Zack Howard, Christophe Cataisson, Val Bliskovski, Jason Winston, Lionel Feigenbaum, Ulrike Lichti, Thomas Ruzicka Triantafyllos Chavakis, and Stuart H. Yuspa. Gene from a Psoriasis Susceptibility Locus Primes the Skin for Inflammation.. Science Translational Medicine. 2010, 2 (61): 61ra90. PMID 21148126. doi:10.1126/scitranslmed.3001108.