Database accession: MF7000606
Name: Human S100A1 with post-translational S-nitrosylation
PDB ID: 2llt
Experimental method: NMR
Assembly: Homodimer
Source organism: Homo sapiens
Primary publication of the structure:
Lenarčič Živković M, Zaręba-Kozioł M, Zhukova L, Poznański J, Zhukov I, Wysłouch-Cieszyńska A
Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein.
(2012) J. Biol. Chem. 287: 40457-70
PMID: 22989881
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
ATPase binding ATPase binding
calcium ion binding calcium ion binding
calcium-dependent protein binding calcium-dependent protein binding
identical protein binding identical protein binding
protein homodimerization activity protein homodimerization activity
S100 protein binding S100 protein binding
Biological process:
intracellular signal transduction intracellular signal transduction
positive regulation of nitric-oxide synthase activity positive regulation of nitric-oxide synthase activity
positive regulation of sprouting angiogenesis positive regulation of sprouting angiogenesis
regulation of heart contraction regulation of heart contraction
substantia nigra development substantia nigra development
Cellular component:
cytoplasm cytoplasm
cytosol cytosol
extracellular region extracellular region
Golgi apparatus Golgi apparatus
mitochondrion mitochondrion
nucleoplasm nucleoplasm
nucleus nucleus
protein-containing complex protein-containing complex
sarcoplasmic reticulum sarcoplasmic reticulum
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
Name: Protein S100-A1
Source organism: Homo sapiens
Length: 94 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
UniProtKB AC: P23297 (positions: 2-94)
Coverage: 98%
Name: Protein S100-A1
Source organism: Homo sapiens
Length: 94 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
UniProtKB AC: P23297 (positions: 2-94)
Coverage: 98%
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:
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). Download the CIF file (.cif)
Download this entry's XML file (.xml)
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