General Information

Database accession: MF7000608

Name: Human S100A14

PDB ID: 2m0r PDBe

Experimental method: NMR

Assembly: Homodimer

Source organism: Homo sapiens

Primary publication of the structure:

Bertini I, Borsi V, Cerofolini L, Das Gupta S, Fragai M, Luchinat C
Solution structure and dynamics of human S100A14.
(2013) J. Biol. Inorg. Chem. 18: 183-194

PMID: 23197251 PubMed

Abstract:

Human S100A14 is a member of the EF-hand calcium-binding protein family that has only recently been described in terms of its functional and pathological properties. The protein is overexpressed in a variety of tumor cells and it has been shown to trigger receptor for advanced glycation end products (RAGE)-dependent signaling in cell cultures. The solution structure of homodimeric S100A14 in the apo state has been solved at physiological temperature. It is shown that the protein does not bind calcium(II) ions and exhibits a "semi-open" conformation that thus represents the physiological structure of the S100A14. The lack of two ligands in the canonical EF-hand calcium(II)-binding site explains the negligible affinity for calcium(II) in solution, and the exposed cysteines and histidine account for the observed precipitation in the presence of zinc(II) or copper(II) ions.


Function and Biology Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.

Molecular function:

calcium ion binding calcium ion binding GeneOntology

calcium-dependent protein binding calcium-dependent protein binding GeneOntology

chemokine receptor binding chemokine receptor binding GeneOntology

Biological process:

apoptotic process apoptotic process GeneOntology

calcium ion homeostasis calcium ion homeostasis GeneOntology

defense response to bacterium defense response to bacterium GeneOntology

positive regulation of granulocyte chemotaxis positive regulation of granulocyte chemotaxis GeneOntology

positive regulation of monocyte chemotaxis positive regulation of monocyte chemotaxis GeneOntology

response to lipopolysaccharide response to lipopolysaccharide GeneOntology

toll-like receptor 4 signaling pathway toll-like receptor 4 signaling pathway GeneOntology

Cellular component:

extracellular exosome extracellular exosome GeneOntology

extracellular space extracellular space GeneOntology

perinuclear region of cytoplasm perinuclear region of cytoplasm GeneOntology

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 2 distinct polypeptide molecules

Chains: A, B

Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.

Number of unique protein segments: 1


Chain A

Name: Protein S100-A14

Source organism: Homo sapiens

Length: 104 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMGQCRSANAEDAQEFSDVERAIETLIKNFHQYSVEGGKETLTPSELRDLVTQQLPHLMPSNCGLEEKIANLGSCNDSKLEFRSFWELIGEAAKSVKLERPVRGH

UniProtKB AC: Q9HCY8 (positions: 1-104) UniProt

Coverage: 100%

Chain B

Name: Protein S100-A14

Source organism: Homo sapiens

Length: 104 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMGQCRSANAEDAQEFSDVERAIETLIKNFHQYSVEGGKETLTPSELRDLVTQQLPHLMPSNCGLEEKIANLGSCNDSKLEFRSFWELIGEAAKSVKLERPVRGH

UniProtKB AC: Q9HCY8 (positions: 1-104) UniProt

Coverage: 100%

Evidence Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding.

Representative domain in related structures: S-100/ICaBP type EF hand dimer

Evidence level: Direct evidence

Evidence coverage: The full structure participates in mutual synergistic folding.

Complex Evidence:

GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface.

Chain A:

N/A

Chain B:

N/A

Surface and contacts features:

Related Structure(s) Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap).

There are 37 related structures in the MFIB database:






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