1uph
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1uph.gif|left|200px]] | + | [[Image:1uph.gif|left|200px]] |
| - | + | ||
| - | '''HIV-1 MYRISTOYLATED MATRIX''' | + | {{Structure |
| + | |PDB= 1uph |SIZE=350|CAPTION= <scene name='initialview01'>1uph</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MYR:MYRISTIC ACID'>MYR</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HIV-1 MYRISTOYLATED MATRIX''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1UPH is a [ | + | 1UPH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_12) Human immunodeficiency virus type 1 (isolate 12)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPH OCA]. |
==Reference== | ==Reference== | ||
| - | Entropic switch regulates myristate exposure in the HIV-1 matrix protein., Tang C, Loeliger E, Luncsford P, Kinde I, Beckett D, Summers MF, Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):517-22. Epub 2003 Dec 29. PMID:[http:// | + | Entropic switch regulates myristate exposure in the HIV-1 matrix protein., Tang C, Loeliger E, Luncsford P, Kinde I, Beckett D, Summers MF, Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):517-22. Epub 2003 Dec 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14699046 14699046] |
[[Category: Human immunodeficiency virus type 1 (isolate 12)]] | [[Category: Human immunodeficiency virus type 1 (isolate 12)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 27: | Line 36: | ||
[[Category: post-translational modification]] | [[Category: post-translational modification]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:06 2008'' |
Revision as of 12:35, 20 March 2008
| |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HIV-1 MYRISTOYLATED MATRIX
Overview
The myristoylated matrix protein (myr-MA) of HIV functions as a regulator of intracellular localization, targeting the Gag precursor polyprotein to lipid rafts in the plasma membrane during virus assembly and dissociating from the membrane during infectivity for nuclear targeting of the preintegration complex. Membrane release is triggered by proteolytic cleavage of Gag, and it has, until now, been believed that proteolysis induces a conformational change in myr-MA that sequesters the myristyl group. NMR studies reported here reveal that myr-MA adopts myr-exposed [myr(e)] and -sequestered [myr(s)] states, as anticipated. Unexpectedly, the tertiary structures of the protein in both states are very similar, with the sequestered myristyl group occupying a cavity that requires only minor conformational adjustments for insertion. In addition, myristate exposure is coupled with trimerization, with the myristyl group sequestered in the monomer and exposed in the trimer (K(assoc) = 2.5 +/- 0.6 x 10(8) M(-2)). The equilibrium constant is shifted approximately 20-fold toward the trimeric, myristate-exposed species in a Gag-like construct that includes the capsid domain, indicating that exposure is enhanced by Gag subdomains that promote self-association. Our findings indicate that the HIV-1 myristyl switch is regulated not by mechanically induced conformational changes, as observed for other myristyl switches, but instead by entropic modulation of a preexisting equilibrium.
About this Structure
1UPH is a Single protein structure of sequence from Human immunodeficiency virus type 1 (isolate 12). Full crystallographic information is available from OCA.
Reference
Entropic switch regulates myristate exposure in the HIV-1 matrix protein., Tang C, Loeliger E, Luncsford P, Kinde I, Beckett D, Summers MF, Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):517-22. Epub 2003 Dec 29. PMID:14699046
Page seeded by OCA on Thu Mar 20 14:35:06 2008
