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(New page: '''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!''' ==This is a placeholder== This is a placeholder text to help you get ...)
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'''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!'''
'''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!'''
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==This is a placeholder==
 
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This is a placeholder text to help you get started in
 
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placing a Jmol applet on your page. At any time, click
 
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"Show Preview" at the bottom of this page to see how it goes.
 
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Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
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Name: Marissa McGarry
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and display another structure.
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{{STRUCTURE_3cin | PDB=3cin | SCENE= }}
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The overall structure of TRAIL is a set of <scene name='Sandbox8/Overall_structure/1'>beta sheets</scene>.
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TRAIL is a newly identified cytokine belonging to the large tumor necrosis factor (TNF) family. TRAIL is a novel molecule inducing apoptosis in a wide variety of tumor cells but not in normal cells. To help in elucidating its biological roles and designing mutants with improved therapeutic potential, we have determined the crystal structure of human TRAIL. The structure reveals that a unique frame insertion of 12-16 amino acids adopts a salient loop structure penetrating into the receptor-binding site. The loop drastically alters the common receptor-binding surface of the TNF family most likely for the specific recognition of cognate partners. A structure-based mutagenesis study demonstrates a critical role of the insertion loop in the cytotoxic activity of TRAIL.
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Reference: 2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity., Cha SS, Kim MS, Choi YH, Sung BJ, Shin NK, Shin HC, Sung YC, Oh BH, Immunity. 1999 Aug;11(2):253-61. PMID:10485660
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{{STRUCTURE_1d2q | PDB=1d2q | SCENE= }}

Revision as of 01:16, 3 March 2009

This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!

Name: Marissa McGarry

The overall structure of TRAIL is a set of .

TRAIL is a newly identified cytokine belonging to the large tumor necrosis factor (TNF) family. TRAIL is a novel molecule inducing apoptosis in a wide variety of tumor cells but not in normal cells. To help in elucidating its biological roles and designing mutants with improved therapeutic potential, we have determined the crystal structure of human TRAIL. The structure reveals that a unique frame insertion of 12-16 amino acids adopts a salient loop structure penetrating into the receptor-binding site. The loop drastically alters the common receptor-binding surface of the TNF family most likely for the specific recognition of cognate partners. A structure-based mutagenesis study demonstrates a critical role of the insertion loop in the cytotoxic activity of TRAIL.

Reference: 2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity., Cha SS, Kim MS, Choi YH, Sung BJ, Shin NK, Shin HC, Sung YC, Oh BH, Immunity. 1999 Aug;11(2):253-61. PMID:10485660


PDB ID 1d2q

Drag the structure with the mouse to rotate
1d2q, resolution 2.80Å ()
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


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