1htn

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[[Image:1htn.gif|left|200px]]<br /><applet load="1htn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1htn.gif|left|200px]]
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caption="1htn, resolution 2.8&Aring;" />
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'''HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL'''<br />
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{{Structure
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|PDB= 1htn |SIZE=350|CAPTION= <scene name='initialview01'>1htn</scene>, resolution 2.8&Aring;
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|SITE= <scene name='pdbsite=CA1:Ca+Binding+Site+1'>CA1</scene> and <scene name='pdbsite=CA2:Ca+Binding+Site+2'>CA2</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=CA1:Ca+Binding+Site+1'>CA1</scene> and <scene name='pdbsite=CA2:Ca+Binding+Site+2'>CA2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTN OCA].
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1HTN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTN OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9256258 9256258]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9256258 9256258]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: tetranectin]]
[[Category: tetranectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:25 2008''

Revision as of 09:41, 20 March 2008

Image:1htn.gif


PDB ID 1htn

Drag the structure with the mouse to rotate
, resolution 2.8Å
Sites: and
Ligands:
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

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