Sandbox8: Difference between revisions
No edit summary |
No edit summary |
||
| (11 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
'''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!''' | ||
==TRAIL (TNF-RELATED APOPTOSIS INDUCING LIGAND)== | |||
Name: Marissa McGarry 03/02/09 | Name: Marissa McGarry 03/02/09 | ||
LKT: 13 beta STRANDS | |||
The overall structure of TRAIL is a set of 13 <scene name='Sandbox8/Overall_structure/1'>beta sheets</scene> (shown in red). As you can see, the exterior of the protein has all of the <scene name='Sandbox8/Negative_and_positive/1'>negative and positive</scene> side chains, as shown in pink. The <scene name='Sandbox8/Aliphatic/1'>amphipathic</scene> elements on the surface of the protein are shown on the beta sheets in green. The polar/charged elements are on the surface of the protein, while the hydrophobic elements are on the inside of the beta sheet. <scene name='Sandbox8/Hydophobic_element/1'>Phe181</scene>, shown in green, is a hydrophobic element on the surface of the protein. | |||
TRAIL is a member of the tumor necrosis factor(TNF) family. TRAIL selectively induces apoptosis in a wide variety of tumor cells but not in normal cells, which gives it promise as a cancer therapeutic. | |||
"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: | Reference: 1d2q proteopedia page | ||
{{STRUCTURE_1d2q | PDB=1d2q | SCENE= }} | {{STRUCTURE_1d2q | PDB=1d2q | SCENE= }} | ||
Latest revision as of 04:47, 20 March 2009
This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!
TRAIL (TNF-RELATED APOPTOSIS INDUCING LIGAND)TRAIL (TNF-RELATED APOPTOSIS INDUCING LIGAND)
Name: Marissa McGarry 03/02/09 LKT: 13 beta STRANDS
The overall structure of TRAIL is a set of 13 (shown in red). As you can see, the exterior of the protein has all of the side chains, as shown in pink. The elements on the surface of the protein are shown on the beta sheets in green. The polar/charged elements are on the surface of the protein, while the hydrophobic elements are on the inside of the beta sheet. , shown in green, is a hydrophobic element on the surface of the protein.
TRAIL is a member of the tumor necrosis factor(TNF) family. TRAIL selectively induces apoptosis in a wide variety of tumor cells but not in normal cells, which gives it promise as a cancer therapeutic.
"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: 1d2q proteopedia page
| |||||||||
| 1d2q, resolution 2.80Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
