1htn
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1htn |SIZE=350|CAPTION= <scene name='initialview01'>1htn</scene>, resolution 2.8Å | |PDB= 1htn |SIZE=350|CAPTION= <scene name='initialview01'>1htn</scene>, resolution 2.8Å | ||
|SITE= <scene name='pdbsite=CA1:Ca+Binding+Site+1'>CA1</scene> and <scene name='pdbsite=CA2:Ca+Binding+Site+2'>CA2</scene> | |SITE= <scene name='pdbsite=CA1:Ca+Binding+Site+1'>CA1</scene> and <scene name='pdbsite=CA2:Ca+Binding+Site+2'>CA2</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1htn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htn OCA], [http://www.ebi.ac.uk/pdbsum/1htn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1htn RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Rasmussen, H.]] | [[Category: Rasmussen, H.]] | ||
[[Category: Thogersen, H C.]] | [[Category: Thogersen, H C.]] | ||
| - | [[Category: CA]] | ||
[[Category: alpha-helical coiled coil]] | [[Category: alpha-helical coiled coil]] | ||
[[Category: c-type lectin]] | [[Category: c-type lectin]] | ||
| Line 38: | Line 40: | ||
[[Category: tetranectin]] | [[Category: tetranectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:15 2008'' |
Revision as of 18:10, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 21:10:15 2008
