4AQJ

Structure of human S100A7 D24G bound to zinc and calcium

Summary for 4AQJ

• Entry DOI: 10.2210/pdb4aqj/pdb
• Related: 1PSR 2PSR 2WND 2WOR 2WOS 3PSR 4AQI
• Descriptor: PROTEIN S100-A7, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: metal binding protein, cancer, inflammation, ef-hand
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P31151
• Total number of polymer chains: 1
• Total formula weight: 12174.57

Authors

Murray, J.I.,Tonkin, M.L.,Whiting, A.L.,Peng, F.,Farnell, B.,Hof, F.,Boulanger, M.J. (deposition date: 2012-04-17, release date: 2012-10-17, Last modification date: 2024-11-20)

Primary citation

Murray, J.I.,Tonkin, M.L.,Whiting, A.L.,Peng, F.,Farnell, B.,Cullen, J.T.,Hof, F.,Boulanger, M.J.
Structural Characterization of S100A15 Reveals a Novel Zinc Coordination Site Among S100 Proteins and Altered Surface Chemistry with Functional Implications for Receptor Binding.
Bmc Struct.Biol., 12:16-, 2012

PubMed Abstract: S100 proteins are a family of small, EF-hand containing calcium-binding signaling proteins that are implicated in many cancers. While the majority of human S100 proteins share 25-65% sequence similarity, S100A7 and its recently identified paralog, S100A15, display 93% sequence identity. Intriguingly, however, S100A7 and S100A15 serve distinct roles in inflammatory skin disease; S100A7 signals through the receptor for advanced glycation products (RAGE) in a zinc-dependent manner, while S100A15 signals through a yet unidentified G-protein coupled receptor in a zinc-independent manner. Of the seven divergent residues that differentiate S100A7 and S100A15, four cluster in a zinc-binding region and the remaining three localize to a predicted receptor-binding surface.

PubMed: 22747601
DOI: 10.1186/1472-6807-12-16

Experimental method

X-RAY DIFFRACTION (1.6 Å)