1htn: Difference between revisions

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.

1HTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: CA1 and CA2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HTN OCA].  

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