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2vx8

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Revision as of 11:50, 23 September 2020

Vamp7 longin domain Hrb peptide complex

Structural highlights

2vx8 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AGFG1_HUMAN] Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

SNAREs provide the specificity and energy for the fusion of vesicles with their target membrane, but how they are sorted into the appropriate vesicles on post-Golgi trafficking pathways is largely unknown. We demonstrate that the clathrin-mediated endocytosis of the SNARE VAMP7 is directly mediated by Hrb, a clathrin adaptor and ArfGAP. Hrb wraps 20 residues of its unstructured C-terminal tail around the folded VAMP7 longin domain, demonstrating that unstructured regions of clathrin adaptors can select cargo. Disrupting this interaction by mutation of the VAMP7 longin domain or depletion of Hrb causes VAMP7 to accumulate on the cell's surface. However, the SNARE helix of VAMP7 binds back onto its longin domain, outcompeting Hrb for binding to the same groove and suggesting that Hrb-mediated endocytosis of VAMP7 occurs only when VAMP7 is incorporated into a cis-SNARE complex. These results elucidate the mechanism of retrieval of a postfusion SNARE complex in clathrin-coated vesicles.

Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb.,Pryor PR, Jackson L, Gray SR, Edeling MA, Thompson A, Sanderson CM, Evans PR, Owen DJ, Luzio JP Cell. 2008 Sep 5;134(5):817-27. PMID:18775314^[4]

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

References

↑ Doria M, Salcini AE, Colombo E, Parslow TG, Pelicci PG, Di Fiore PP. The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport. J Cell Biol. 1999 Dec 27;147(7):1379-84. PMID:10613896
↑ Sanchez-Velar N, Udofia EB, Yu Z, Zapp ML. hRIP, a cellular cofactor for Rev function, promotes release of HIV RNAs from the perinuclear region. Genes Dev. 2004 Jan 1;18(1):23-34. Epub 2003 Dec 30. PMID:14701878 doi:10.1101/gad.1149704
↑ Yu Z, Sanchez-Velar N, Catrina IE, Kittler EL, Udofia EB, Zapp ML. The cellular HIV-1 Rev cofactor hRIP is required for viral replication. Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):4027-32. Epub 2005 Mar 4. PMID:15749819 doi:http://dx.doi.org/0408889102
↑ Pryor PR, Jackson L, Gray SR, Edeling MA, Thompson A, Sanderson CM, Evans PR, Owen DJ, Luzio JP. Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb. Cell. 2008 Sep 5;134(5):817-27. PMID:18775314 doi:10.1016/j.cell.2008.07.023

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vx8"

@@ Line 1: / Line 1: @@
 ==Vamp7 longin domain Hrb peptide complex==
-<StructureSection load='2vx8' size='340' side='right' caption='[[2vx8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='2vx8' size='340' side='right'caption='[[2vx8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vx8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VX8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vx8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VX8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VX8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2vx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vx8 OCA], [http://pdbe.org/2vx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vx8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vx8 ProSAT]</span></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=2vx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vx8 OCA], [http://pdbe.org/2vx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vx8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vx8 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Evans, P R]]
 [[Category: Luzio, J P]]

2vx8

From Proteopedia

Revision as of 11:50, 23 September 2020

Vamp7 longin domain Hrb peptide complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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