2jmg

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of V7R mutant of HIV-1 myristoylated matrix protein

Structural highlights

2jmg is a 1 chain structure with sequence from Human immunodeficiency virus 1. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6E183_9HIV1

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

During the late phase of human immunodeficiency virus type-1 (HIV-1) replication, newly synthesized retroviral Gag proteins are targeted to lipid raft regions of specific cellular membranes, where they assemble and bud to form new virus particles. Gag binds preferentially to the plasma membrane (PM) of most hematopoietic cell types, a process mediated by interactions between the cellular PM marker phosphatidylinositol-(4,5)-bisphosphate (PI(4,5)P(2)) and Gag's N-terminally myristoylated matrix (MA) domain. We recently demonstrated that PI(4,5)P(2) binds to a conserved cleft on MA and promotes myristate exposure, suggesting a role as both a direct membrane anchor and myristyl switch trigger. Here we show that PI(4,5)P(2) is also capable of binding to MA proteins containing point mutations that inhibit membrane binding in vitro, and in vivo, including V7R, L8A and L8I. However, these mutants do not exhibit PI(4,5)P(2) or concentration-dependent myristate exposure. NMR studies of V7R and L8A MA reveal minor structural changes that appear to be responsible for stabilizing the myristate-sequestered (myr(s)) species and inhibiting exposure. Unexpectedly, the myristyl group of a revertant mutant with normal PM targeting properties (V7R,L21K) is also tightly sequestered and insensitive to PI(4,5)P(2) binding. This mutant binds PI(4,5)P(2) with twofold higher affinity compared with the native protein, suggesting a potential compensatory mechanism for membrane binding.

Point mutations in the HIV-1 matrix protein turn off the myristyl switch.,Saad JS, Loeliger E, Luncsford P, Liriano M, Tai J, Kim A, Miller J, Joshi A, Freed EO, Summers MF J Mol Biol. 2007 Feb 16;366(2):574-85. Epub 2006 Dec 1. PMID:17188710^[1]

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

References

↑ Saad JS, Loeliger E, Luncsford P, Liriano M, Tai J, Kim A, Miller J, Joshi A, Freed EO, Summers MF. Point mutations in the HIV-1 matrix protein turn off the myristyl switch. J Mol Biol. 2007 Feb 16;366(2):574-85. Epub 2006 Dec 1. PMID:17188710 doi:10.1016/j.jmb.2006.11.068

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Solution structure of V7R mutant of HIV-1 myristoylated matrix protein==
-<StructureSection load='2jmg' size='340' side='right' caption='[[2jmg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2jmg' size='340' side='right'caption='[[2jmg]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jmg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JMG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2jmg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JMG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h3i|2h3i]], [[2nv3|2nv3]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</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=2jmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmg OCA], [https://pdbe.org/2jmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jmg RCSB], [https://www.ebi.ac.uk/pdbsum/2jmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmg ProSAT]</span></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=2jmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmg OCA], [http://pdbe.org/2jmg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jmg RCSB], [http://www.ebi.ac.uk/pdbsum/2jmg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q72497_9HIV1 Q72497_9HIV1]] Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS012344_004_011858]
+[https://www.uniprot.org/uniprot/Q6E183_9HIV1 Q6E183_9HIV1]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/2jmg_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 32: / Line 31: @@
 ==See Also==
-*[[Gag polyprotein|Gag polyprotein]]
+*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Freed, E O]]
+[[Category: Human immunodeficiency virus 1]]
-[[Category: Joshi, A]]
+[[Category: Large Structures]]
-[[Category: Kim, A]]
+[[Category: Freed EO]]
-[[Category: Liriano, M]]
+[[Category: Joshi A]]
-[[Category: Loeliger, E]]
+[[Category: Kim A]]
-[[Category: Luncsford, P]]
+[[Category: Liriano M]]
-[[Category: Miller, J]]
+[[Category: Loeliger E]]
-[[Category: Saad, J S]]
+[[Category: Luncsford P]]
-[[Category: Summers, M F]]
+[[Category: Miller J]]
-[[Category: Tai, J]]
+[[Category: Saad JS]]
-[[Category: V7r mutant of hiv-1 myristoylated matrix protein]]
+[[Category: Summers MF]]
-[[Category: Viral protein]]
+[[Category: Tai J]]

2jmg

From Proteopedia

Current revision

Solution structure of V7R mutant of HIV-1 myristoylated matrix protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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