PDBsum entry 2m1k

Protein binding

PDB id: 2m1k

Contents

Protein chains

89 a.a.

101 a.a.

PDB id:

2m1k

Name:

Protein binding

Title:

Interaction of human s100a6 (c3s) with v domain of receptor for advanced glycation end products (rage)

Structure:

Protein s100-a6. Chain: b, d. Synonym: calcyclin, growth factor-inducible protein 2a9, mln 4, prolactin receptor-associated protein, pra, s100 calcium-binding protein a6. Engineered: yes. Mutation: yes. Advanced glycosylation end product-specific receptor. Chain: a, c.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: cacy, s100a6. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: ager, rage.

NMR struc:

20 models

Authors:

A.A.Gupta,C.Yu

Key ref:

S.K.Mohan et al. (2013). Interaction of the S100A6 mutant (C3S) with the V domain of the receptor for advanced glycation end products (RAGE). Biochem Biophys Res Commun, 434, 328-333. PubMed id: 23537648 DOI: 10.1016/j.bbrc.2013.03.049

Date:

29-Nov-12 Release date: 25-Mar-15

Protein chains

P06703  (S10A6_HUMAN) -  Protein S100-A6 from Homo sapiens

Seq: 90 a.a.

Struc: 89 a.a.*

Protein chains

Q15109  (RAGE_HUMAN) -  Advanced glycosylation end product-specific receptor from Homo sapiens

Seq: 404 a.a.

Struc: 101 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/j.bbrc.2013.03.049

Biochem Biophys Res Commun 434:328-333 (2013)

PubMed id: 23537648

Interaction of the S100A6 mutant (C3S) with the V domain of the receptor for advanced glycation end products (RAGE).

S.K.Mohan, A.A.Gupta, C.Yu.

ABSTRACT

S100A6 is involved in several vital biological functions, such as calcium sensing and cell proliferation. It is a homodimeric protein that belongs to the S100 protein family. The receptor for advanced glycation end products (RAGE) has been shown to play a role in the progression of various disease conditions, such as diabetes and immune/inflammatory disorders. Information regarding the association of RAGE with S100 proteins at a molecular level is useful to understand the diversity of the RAGE signaling pathways. In this report, biomolecular NMR techniques were utilized for the resonance assignment of the C3S mutation in human S100A6 and characterizing its interaction with the RAGE V domain. Further binding affinity between S100A6m and the RAGE V domain was determined by isothermal titration calorimetric studies. HADDOCK was used to generate a heterotetramer model of the S100A6m-RAGE V domain complex. This model provides an important insights into the S100-RAGE cellular signaling pathway.