1htn
From Proteopedia
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[[Image:1htn.gif|left|200px]] | [[Image:1htn.gif|left|200px]] | ||
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'''HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL''' | '''HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL''' | ||
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[[Category: Rasmussen, H.]] | [[Category: Rasmussen, H.]] | ||
[[Category: Thogersen, H C.]] | [[Category: Thogersen, H C.]] | ||
- | [[Category: | + | [[Category: Alpha-helical coiled coil]] |
- | [[Category: | + | [[Category: C-type lectin]] |
- | [[Category: | + | [[Category: Carbohydrate recognition domain]] |
- | [[Category: | + | [[Category: Kringle 4]] |
- | [[Category: | + | [[Category: Plasminogen binding]] |
- | [[Category: | + | [[Category: Tetranectin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:13:09 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 16:13, 2 May 2008
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 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.
About this Structure
1HTN is a Single protein structure of sequence from Homo sapiens. 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 Fri May 2 19:13:09 2008