General Information

Database Accession: DI2010011

Name: Annexin II bound to S100A10 dimer

PDB ID: 1bt6 PDB

Experimental method: X-ray (2.40 Å)

Source organism: Gallus gallus / Homo sapiens

Proof of disorder: Inferred from homology

Primary publication of the structure:

Réty S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A
The crystal structure of a complex of p11 with the annexin II N-terminal peptide.
(1999) Nat. Struct. Biol. 6: 89-95

PMID: 9886297 PubMed

Abstract:

The aggregation and membrane fusion properties of annexin II are modulated by the association with a regulatory light chain called p11.p11 is a member of the S100 EF-hand protein family, which is unique in having lost its calcium-binding properties. We report the first structure of a complex between p11 and its cognate peptide, the N-terminus of annexin II, as well as that of p11 alone. The basic unit for p11 is a tight, non-covalent dimer. In the complex, each annexin II peptide forms hydrophobic interactions with both p11 monomers, thus providing a structural basis for high affinity interactions between an S100 protein and its target sequence. Finally, p11 forms a disulfide-linked tetramer in both types of crystals thus suggesting a model for an oxidized form of other S100 proteins that have been found in the extracellular milieu.

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 Interacting selectively and non-covalently with calcium ions (Ca2+). GeneOntology

protein binding Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). GeneOntology

Biological process:

transport The directed movement of substances (such as macromolecules, small molecules, ions) or cellular components (such as complexes and organelles) into, out of or within a cell, or between cells, or within a multicellular organism by means of some agent such as a transporter, pore or motor protein. GeneOntology

regulation of catalytic activity Any process that modulates the activity of an enzyme. GeneOntology

positive regulation of cell differentiation Any process that activates or increases the frequency, rate or extent of cell differentiation. GeneOntology

Cellular component:

plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GeneOntology

vesicle Any small, fluid-filled, spherical organelle enclosed by membrane. GeneOntology

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 3 distinct polypeptide molecules

Chains: C, A, B

Notes: Chain D was removed as chains A, B and C highlight the biologically relevant interaction.

Chain C

Name: Annexin A2 Disordered Inferred from homology

Source organism: Gallus gallus

Length: 14 residues

Sequence:Sequence according to PDB SEQRESMSTVHEILSKLSLE

UniProtKB AC: P17785 (positions: 1-14) UniProt Coverage: 4.1%

UniRef90 AC: UniRef90_P07356 (positions: 2-14) UniRef90

Chain A

Name: Protein S100-A10 Ordered component

Source organism: Homo sapiens

Length: 96 residues

Sequence:Sequence according to PDB SEQRESPSQMEHAMETMMFTFHKFAGDKGYLTKEDLRVLMEKEFPGFLENQKDPLAVDKIMKDLDQCRDGKVGFQSFFSLIAGLTIACNDYFVVHMKQKGKK

UniProtKB AC: P60903 (positions: 2-97) UniProt Coverage: 99%

UniRef90 AC: UniRef90_P60903 (positions: 2-97) UniRef90

Chain B

Name: Protein S100-A10 Ordered component

Source organism: Homo sapiens

Length: 96 residues

Sequence:Sequence according to PDB SEQRESPSQMEHAMETMMFTFHKFAGDKGYLTKEDLRVLMEKEFPGFLENQKDPLAVDKIMKDLDQCRDGKVGFQSFFSLIAGLTIACNDYFVVHMKQKGKK

UniProtKB AC: P60903 (positions: 2-97) UniProt Coverage: 99%

UniRef90 AC: UniRef90_P60903 (positions: 2-97) UniRef90

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

Chain C: Disordered Inferred from homology

The interacting region of a closely homologous protein has been shown to be highly flexible corresponding to missing coordinates in X-ray structures (PDB IDs: 1w7b, 4x9p).

Chain A: Ordered component

S100A is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF01023). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4p.

Chain B: Ordered component

S100A is known to adopt a stable structure in isolation in dimeric form (see Pfam domain PF01023). A solved structure of the domain dimer without bound ligands is represented by PDB ID 1a4p.

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).

No related structure was found in the Protein Data Bank.

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