1HTN

HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL

Summary for 1HTN

• Entry DOI: 10.2210/pdb1htn/pdb
• Descriptor: TETRANECTIN, CALCIUM ION (3 entities in total)
• Functional Keywords: tetranectin, plasminogen binding, kringle 4, alpha-helical coiled coil, c-type lectin, carbohydrate recognition domain, lectin
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 20346.11

Authors

Nielsen, B.B.,Kastrup, J.S.,Rasmussen, H.,Holtet, T.L.,Graversen, J.H.,Etzerodt, M.,Thogersen, H.C.,Larsen, I.K. (deposition date: 1997-05-28, release date: 1997-12-03, Last modification date: 2024-10-30)

Primary citation

Nielsen, B.B.,Kastrup, J.S.,Rasmussen, H.,Holtet, T.L.,Graversen, J.H.,Etzerodt, M.,Thogersen, H.C.,Larsen, I.K.
Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil.
FEBS Lett., 412:388-396, 1997

PubMed 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.

PubMed: 9256258
DOI: 10.1016/S0014-5793(97)00664-9

Experimental method

X-RAY DIFFRACTION (2.8 Å)