› 2v37

Solution NMR

Solution structure of the N-terminal extracellular domain of human T- cadherin

Released:
DOI: 10.2210/pdb2v37/pdb
PDB entry 2v37 coloured by chain, ensemble of 20 models, front view.
PDB entry 2v37 coloured by chain, ensemble of 20 models, side view.
PDB entry 2v37 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain.
Dames SA, Bang E, Haüssinger D, Ahrens T, Engel J, Grzesiek S
J Biol Chem 283 23485-95 (2008)
PMID: 18550521

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cadherin-13 Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55290 (Residues: 139-243; Coverage: 15%)
Gene names: CDH13, CDHH
Sequence domains: Cadherin domain
Structure domains: Cadherins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: X-PLOR-NIH
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Involvement of members of the cadherin superfamily in cancer.
Berx et al. (2009)
6 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)