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5f7t

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Revision as of 08:03, 29 April 2020

TRIM5 B-box2 and coiled-coil chimera

Structural highlights

5f7t is a 4 chain structure with sequence from Macmu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	TRIM5 (MACMU)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRIM5_MACMU] Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV-agm).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Restriction factors and pattern recognition receptors are important components of intrinsic cellular defenses against viral infection. Mammalian TRIM5alpha proteins are restriction factors and receptors that target the capsid cores of retroviruses and activate ubiquitin-dependent antiviral responses upon capsid recognition. Here, we report crystallographic and functional studies of the TRIM5alpha B-box 2 domain, which mediates higher-order assembly of TRIM5 proteins. The B-box can form both dimers and trimers, and the trimers can link multiple TRIM5alpha proteins into a hexagonal net that matches the lattice arrangement of capsid subunits and enables avid capsid binding. Two modes of conformational flexibility allow TRIM5alpha to accommodate the variable curvature of retroviral capsids. B-box mediated interactions also modulate TRIM5alpha's E3 ubiquitin ligase activity, by stereochemically restricting how the N-terminal RING domain can dimerize. Overall, these studies define important molecular details of cellular recognition of retroviruses, and how recognition links to downstream processes to disable the virus.

Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5alpha.,Wagner JM, Roganowicz MD, Skorupka K, Alam SL, Christensen DE, Doss GL, Wan Y, Frank GA, Ganser-Pornillos BK, Sundquist WI, Pornillos O Elife. 2016 Jun 2;5. pii: e16309. doi: 10.7554/eLife.16309. PMID:27253059^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lienlaf M, Hayashi F, Di Nunzio F, Tochio N, Kigawa T, Yokoyama S, Diaz-Griffero F. Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by TRIM5alpha(rh): structure of the RING domain of TRIM5alpha. J Virol. 2011 Sep;85(17):8725-37. Epub 2011 Jul 6. PMID:21734049 doi:10.1128/JVI.00497-11
↑ Tareen SU, Emerman M. Human Trim5alpha has additional activities that are uncoupled from retroviral capsid recognition. Virology. 2011 Jan 5;409(1):113-20. doi: 10.1016/j.virol.2010.09.018. Epub 2010, Oct 28. PMID:21035162 doi:10.1016/j.virol.2010.09.018
↑ Nakayama EE, Shioda T. TRIM5alpha and Species Tropism of HIV/SIV. Front Microbiol. 2012;3:13. doi: 10.3389/fmicb.2012.00013. Epub 2012 Jan 24. PMID:22291694 doi:10.3389/fmicb.2012.00013
↑ Wagner JM, Roganowicz MD, Skorupka K, Alam SL, Christensen DE, Doss GL, Wan Y, Frank GA, Ganser-Pornillos BK, Sundquist WI, Pornillos O. Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5alpha. Elife. 2016 Jun 2;5. pii: e16309. doi: 10.7554/eLife.16309. PMID:27253059 doi:http://dx.doi.org/10.7554/eLife.16309

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5f7t"

@@ Line 1: / Line 1: @@
 ==TRIM5 B-box2 and coiled-coil chimera==
-<StructureSection load='5f7t' size='340' side='right' caption='[[5f7t]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
+<StructureSection load='5f7t' size='340' side='right'caption='[[5f7t]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5f7t]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F7T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5f7t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Macmu Macmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F7T FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7t OCA], [http://pdbe.org/5f7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f7t RCSB], [http://www.ebi.ac.uk/pdbsum/5f7t PDBsum]</span></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRIM5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9544 MACMU])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7t OCA], [http://pdbe.org/5f7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f7t RCSB], [http://www.ebi.ac.uk/pdbsum/5f7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7t ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
+[[Category: Macmu]]
 [[Category: Doss, G]]
 [[Category: Pornillos, O]]

5f7t

From Proteopedia

Revision as of 08:03, 29 April 2020

TRIM5 B-box2 and coiled-coil chimera

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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