Format

Send to

Choose Destination
FEBS Lett. 1997 Jul 28;412(2):388-96.

Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil.

Author information

1
Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Copenhagen. bettina@medchem.dfh.dk

Abstract

Tetranectin is a plasminogen kringle 4-binding protein. The crystal structure has been determined at 2.8 A resolution using molecular replacement. Human tetranectin is a homotrimer forming a triple alpha-helical coiled coil. Each monomer consists of a carbohydrate recognition domain (CRD) connected to a long alpha-helix. Tetranectin has been classified in a distinct group of the C-type lectin superfamily but has structural similarity to the proteins in the group of collectins. Tetranectin has three intramolecular disulfide bridges. Two of these are conserved in the C-type lectin superfamily, whereas the third is present only in long-form CRDs. Tetranectin represents the first structure of a long-form CRD with intact calcium-binding sites. In tetranectin, the third disulfide bridge tethers the CRD to the long helix in the coiled coil. The trimerization of tetranectin as well as the fixation of the CRDs relative to the helices in the coiled coil indicate a demand for high specificity in the recognition and binding of ligands.

PMID:
9256258
DOI:
10.1016/s0014-5793(97)00664-9
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center