1htn
From Proteopedia
|
HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL
Overview
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 ... [(full description)]
About this Structure
1HTN is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Structure known Active Sites: CA1 and CA2. Full crystallographic information is available from [OCA].
Reference
Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil., Nielsen BB, Kastrup JS, Rasmussen H, Holtet TL, Graversen JH, Etzerodt M, Thogersen HC, Larsen IK, FEBS Lett. 1997 Jul 28;412(2):388-96. PMID:9256258
Page seeded by OCA on Tue Oct 30 15:38:43 2007
Categories: Homo sapiens | Single protein | Etzerodt, M. | Graversen, J.H. | Holtet, T.L. | Kastrup, J.S. | Larsen, I.K. | Nielsen, B.B. | Rasmussen, H. | Thogersen, H.C. | CA | Alpha-helical coiled coil | C-type lectin | Carbohydrate recognition domain | Kringle 4 | Plasminogen binding | Tetranectin
