TRAIL: Difference between revisions

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<StructureSection load='1d0g' size='340' side='right' caption='Human TRAIL trimer residues 114-281 (grey, light green, yellow) complex with death receptor-5 extracellular domain (dark blue, dark green, olive), Zn+2 (grey) and Cl-1 (green) ions, [[1d0g]]' scene='' pspeed='8'>
<StructureSection load='1d0g' size='340' side='right' caption='Human TRAIL trimer residues 114-281 (grey, light green, yellow) complex with death receptor-5 extracellular domain (dark blue, dark green, olive), Zn+2 (grey) and Cl-1 (green) ions, [[1d0g]]' scene='' pspeed='8'>
== Function ==
== Function ==
'''TRAIL (TNF-related apoptosis-inducing ligand)''' functions as a ligand in the process of apoptosis<ref>PMID:15987601</ref>.  TRAIL binds to death receptors DR4, DR5, DcR1 and DcR2.  For details see [[Molecular Playground/TRAIL]]. <scene name='48/480878/Cv/1'>TRAIL trimer residues complex with death receptor-5 extracellular domain</scene> ([[1d0g]]). <scene name='48/480878/Cv/2'>Zn+2 and Cl-1 bind to 3 same Cys residues from different subunits of TRAIL trimer</scene>.  
'''TRAIL (TNF-related apoptosis-inducing ligand)''' or '''TNF ligand superfamily 10''' functions as a ligand in the process of apoptosis<ref>PMID:15987601</ref>.  TRAIL binds to death receptors DR4, DR5, DcR1 and DcR2.  For details see [[Molecular Playground/TRAIL]]. <scene name='48/480878/Cv/1'>TRAIL trimer residues complex with death receptor-5 extracellular domain</scene> ([[1d0g]]). <scene name='48/480878/Cv/2'>Zn+2 and Cl-1 bind to 3 same Cys residues from different subunits of TRAIL trimer</scene>.  


== Disease ==
== Disease ==
TRAIL concentrations are reduced in rheumatoid arithritis<ref>PMID:25962765</ref>.
TRAIL concentrations are reduced in rheumatoid arthritis<ref>PMID:25962765</ref>.
</StructureSection>
</StructureSection>
== 3D Structures of TRAIL ==
== 3D Structures of TRAIL ==


[[1d0g]], [[1d4v]], [[1du3]] - hTRAIL residues 114-281 + DR5 extracellular domain - human<br />
[[1d0g]], [[1d4v]], [[1du3]], [[5cir]] - hTRAIL extracellular domain + DR5 extracellular domain - human<br />
[[1dg6]] – hTRAIL jelly-roll domain<br />
[[1dg6]] – hTRAIL jelly-roll domain<br />
[[1d2q]] - hTRAIL extracellular domain
[[1d2q]] - hTRAIL extracellular domain<br />
[[4n90]] - hTRAIL extracellular domain + DR5 extracellular domain + antibody<br />
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 01:05, 11 October 2017

Function

TRAIL (TNF-related apoptosis-inducing ligand) or TNF ligand superfamily 10 functions as a ligand in the process of apoptosis[1]. TRAIL binds to death receptors DR4, DR5, DcR1 and DcR2. For details see Molecular Playground/TRAIL. (1d0g). .

Disease

TRAIL concentrations are reduced in rheumatoid arthritis[2].

Human TRAIL trimer residues 114-281 (grey, light green, yellow) complex with death receptor-5 extracellular domain (dark blue, dark green, olive), Zn+2 (grey) and Cl-1 (green) ions, 1d0g

Drag the structure with the mouse to rotate

3D Structures of TRAIL3D Structures of TRAIL

1d0g, 1d4v, 1du3, 5cir - hTRAIL extracellular domain + DR5 extracellular domain - human
1dg6 – hTRAIL jelly-roll domain
1d2q - hTRAIL extracellular domain
4n90 - hTRAIL extracellular domain + DR5 extracellular domain + antibody

ReferencesReferences

  1. Daniels RA, Turley H, Kimberley FC, Liu XS, Mongkolsapaya J, Ch'En P, Xu XN, Jin BQ, Pezzella F, Screaton GR. Expression of TRAIL and TRAIL receptors in normal and malignant tissues. Cell Res. 2005 Jun;15(6):430-8. PMID:15987601 doi:http://dx.doi.org/10.1038/sj.cr.7290311
  2. Dessein PH, Lopez-Mejias R, Ubilla B, Genre F, Corrales A, Hernandez JL, Ferraz-Amaro I, Tsang L, Pina T, Llorca J, Blanco R, Gonzalez-Juanatey C, Gonzalez-Gay MA. TNF-related apoptosis-inducing ligand and cardiovascular disease in rheumatoid arthritis. Clin Exp Rheumatol. 2015 Jul-Aug;33(4):491-7. Epub 2015 May 11. PMID:25962765

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky