2lm7: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: '''Unreleased structure''' The entry 2lm7 is ON HOLD Authors: Elaid, S., Libersou, S., Ouldali, M., Rhayyat, R., Henry, C., Morellet, N., Lepault, J., Bouaziz, S. Description: NMR stru...
 
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 2lm7 is ON HOLD
==NMR structure of the C-terminal domain of VP7 in membrane mimicking micelles==
<StructureSection load='2lm7' size='340' side='right'caption='[[2lm7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lm7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rotavirus_A_human/BEL/4106/2000_G3P1114 Rotavirus A human/BEL/4106/2000 G3P1114]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LM7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lm7 OCA], [https://pdbe.org/2lm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lm7 RCSB], [https://www.ebi.ac.uk/pdbsum/2lm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lm7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VP7_ROT41 VP7_ROT41] Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In integrin-dependent strains, VP7 seems to essentially target the integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 at a postbinding stage, once the initial attachment by VP4 has been achieved (By similarity).


Authors: Elaid, S., Libersou, S., Ouldali, M., Rhayyat, R., Henry, C., Morellet, N., Lepault, J., Bouaziz, S.
==See Also==
 
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
Description: NMR structure of the C-terminal domain of VP7 in membrane mimicking micelles
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Bouaziz S]]
[[Category: Elaid S]]
[[Category: Lepault J]]
[[Category: Libersou S]]
[[Category: Morellet N]]
[[Category: Ouldali M]]

Latest revision as of 16:09, 26 July 2023

NMR structure of the C-terminal domain of VP7 in membrane mimicking micellesNMR structure of the C-terminal domain of VP7 in membrane mimicking micelles

Structural highlights

2lm7 is a 1 chain structure with sequence from Rotavirus A human/BEL/4106/2000 G3P1114. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VP7_ROT41 Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In integrin-dependent strains, VP7 seems to essentially target the integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 at a postbinding stage, once the initial attachment by VP4 has been achieved (By similarity).

See Also

Drag the structure with the mouse to rotate

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

OCA