General Information

Database accession: MF2100013 Original MFIB entry

Name: S100B

PDB ID: 1uwo PDBe

Experimental method: NMR

Assembly: Homodimer

Source organism: Homo sapiens

Primary publication of the structure:

Smith SP, Shaw GS
A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.
(1998) Structure 6: 211-22

PMID: 9519411 PubMed

Abstract:

Not available.


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

identical protein binding identical protein binding GeneOntology

protein homodimerization activity protein homodimerization activity GeneOntology

RAGE receptor binding RAGE receptor binding GeneOntology

S100 protein binding S100 protein binding GeneOntology

tau protein binding tau protein binding GeneOntology

zinc ion binding zinc ion binding GeneOntology

Biological process:

adaptive thermogenesis adaptive thermogenesis GeneOntology

axonogenesis axonogenesis GeneOntology

cell adhesion cell adhesion GeneOntology

central nervous system development central nervous system development GeneOntology

learning or memory learning or memory GeneOntology

memory memory GeneOntology

positive regulation of canonical NF-kappaB signal transduction positive regulation of canonical NF-kappaB signal transduction GeneOntology

positive regulation of cell population proliferation positive regulation of cell population proliferation GeneOntology

positive regulation of neuron differentiation positive regulation of neuron differentiation GeneOntology

regulation of neuronal synaptic plasticity regulation of neuronal synaptic plasticity GeneOntology

sympathetic neuron projection extension sympathetic neuron projection extension GeneOntology

Cellular component:

cytoplasm cytoplasm GeneOntology

cytosol cytosol GeneOntology

extracellular region extracellular region GeneOntology

extracellular space extracellular space GeneOntology

intracellular membrane-bounded organelle intracellular membrane-bounded organelle GeneOntology

neuronal cell body neuronal cell body GeneOntology

nucleoplasm nucleoplasm GeneOntology

nucleus nucleus GeneOntology

perinuclear region of cytoplasm perinuclear region of cytoplasm GeneOntology

ruffle ruffle 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-B

Source organism: Homo sapiens

Length: 92 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE

UniProtKB AC: P04271 (positions: 2-92) UniProt

Coverage: 98%

Chain B

Name: Protein S100-B

Source organism: Homo sapiens

Length: 92 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE

UniProtKB AC: P04271 (positions: 2-92) UniProt

Coverage: 98%

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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