2LNS

Solution structure of AGR2 residues 41-175

Summary for 2LNS

• Entry DOI: 10.2210/pdb2lns/pdb
• Related: 2LNT
• NMR Information: BMRB: 18178
• Descriptor: Anterior gradient protein 2 homolog (1 entity in total)
• Functional Keywords: anterior-gradient protein 2, thioredoxin-fold, cancer, adhesion, metastasis, isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: O95994
• Total number of polymer chains: 2
• Total formula weight: 32377.17

Authors

Patel, P.,Clarke, C.J.,Barraclough, D.L.,Rudland, P.S.,Barraclough, R.,Lian, L. (deposition date: 2012-01-04, release date: 2013-01-09, Last modification date: 2024-05-15)

Primary citation

Patel, P.,Clarke, C.,Barraclough, D.L.,Jowitt, T.A.,Rudland, P.S.,Barraclough, R.,Lian, L.Y.
Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion.
J.Mol.Biol., 425:929-943, 2013

PubMed Abstract: Anterior gradient 2 (AGR2) is a normal endoplasmic reticulum protein that has two important abnormal functions, amphibian limb regeneration and human cancer metastasis promotion. These normal intracellular and abnormal extracellular roles can be attributed to the multidomain structure of AGR2. The NMR structure shows that AGR2 consists of an unstructured N-terminal region followed by a thioredoxin fold. The protein exists in monomer-dimer equilibrium with a K(d) of 8.83μM, and intermolecular salt bridges involving E60 and K64 within the folded domain serve to stabilize the dimer. The unstructured region is primarily responsible for the ability of AGR2 to promote cell adhesion, while dimerization is less important for this activity. The structural data of AGR2 show a separation between potential catalytic redox activity and adhesion function within the context of metastasis and development.

PubMed: 23274113
DOI: 10.1016/j.jmb.2012.12.009

Experimental method

SOLUTION NMR