5HLO

Crystal structure of calcium and zinc-bound human S100A8 in space group C2221

Summary for 5HLO

• Entry DOI: 10.2210/pdb5hlo/pdb
• Descriptor: Protein S100-A8, CALCIUM ION, ZINC ION, ... (7 entities in total)
• Functional Keywords: s100 protein, calcium, zinc, oligomer, signaling protein
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted: P05109
• Total number of polymer chains: 4
• Total formula weight: 45336.10

Authors

Lin, H.,Andersen, G.R.,Yatime, L. (deposition date: 2016-01-15, release date: 2016-06-08, Last modification date: 2024-01-10)

Primary citation

Lin, H.,Andersen, G.R.,Yatime, L.
Crystal structure of human S100A8 in complex with zinc and calcium.
Bmc Struct.Biol., 16:8-8, 2016

PubMed Abstract: S100 proteins are a large family of calcium binding proteins present only in vertebrates. They function intra- and extracellularly both as regulators of homeostatic processes and as potent effectors during inflammation. Among these, S100A8 and S100A9 are two major constituents of neutrophils that can assemble into homodimers, heterodimers and higher oligomeric species, including fibrillary structures found in the ageing prostate. Each of these forms assumes specific functions and their formation is dependent on divalent cations, notably calcium and zinc. In particular, zinc appears as a major regulator of S100 protein function in a disease context. Despite this central role, no structural information on how zinc bind to S100A8/S100A9 and regulates their quaternary structure is yet available.

PubMed: 27251136
DOI: 10.1186/s12900-016-0058-4

Experimental method

X-RAY DIFFRACTION (2.1 Å)