2gol: Difference between revisions
New page: left|200px<br /> <applet load="2gol" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gol, resolution 2.20Å" /> '''Xray Structure of G... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2gol.gif|left|200px]]<br /> | [[Image:2gol.gif|left|200px]]<br /><applet load="2gol" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2gol" size=" | |||
caption="2gol, resolution 2.20Å" /> | caption="2gol, resolution 2.20Å" /> | ||
'''Xray Structure of Gag278'''<br /> | '''Xray Structure of Gag278'''<br /> | ||
==Overview== | ==Overview== | ||
Gag, the major structural protein of retroviruses such as HIV-1, comprises | Gag, the major structural protein of retroviruses such as HIV-1, comprises a series of domains connected by flexible linkers. These domains drive viral assembly by mediating multiple interactions between adjacent Gag molecules and by binding to viral genomic RNA and host cell membranes. Upon viral budding, Gag is processed by the viral protease to liberate distinct domains as separate proteins. The first two regions of Gag are MA, a membrane-binding module, and CA, which is a two-domain protein that makes important Gag-Gag interactions, forms the cone-shaped outer shell of the core (the capsid) in the mature HIV-1 particle, and makes an important interaction with the cellular protein cyclophilin A (CypA). Here, we report crystal structures of the mature CA N-terminal domain (CA(N)(133-278)) and a MA-CA(N) fusion (Gag(1-278)) at resolutions/R(free) values of 1.9 A/25.7% and 2.2 A/25.8%, respectively. Consistent with earlier studies, a comparison of these structures indicates that processing at the MA-CA junction causes CA to adopt an N-terminal beta-hairpin conformation that seems to be required for capsid morphology and viral infectivity. In contrast with an NMR study (Tang, C., et al. (2002) Nat. Struct. Biol. 9, 537-543), structural overlap reveals only small relative displacements for helix 6, which is located between the beta-hairpin and the CypA-binding loop. These observations argue against the proposal that CypA binding is coupled with beta-hairpin formation and support an earlier surface plasmon resonance study (Yoo, S., et al. (1997) J. Mol. Biol. 269, 780-795), which concluded that beta-hairpin formation and CypA-binding are energetically independent events. | ||
==About this Structure== | ==About this Structure== | ||
2GOL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2GOL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GOL OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Kelly, B | [[Category: Kelly, B N.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: gag]] | [[Category: gag]] | ||
| Line 21: | Line 20: | ||
[[Category: viral maturation]] | [[Category: viral maturation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:42 2008'' | ||
Revision as of 18:33, 21 February 2008
|
Xray Structure of Gag278
OverviewOverview
Gag, the major structural protein of retroviruses such as HIV-1, comprises a series of domains connected by flexible linkers. These domains drive viral assembly by mediating multiple interactions between adjacent Gag molecules and by binding to viral genomic RNA and host cell membranes. Upon viral budding, Gag is processed by the viral protease to liberate distinct domains as separate proteins. The first two regions of Gag are MA, a membrane-binding module, and CA, which is a two-domain protein that makes important Gag-Gag interactions, forms the cone-shaped outer shell of the core (the capsid) in the mature HIV-1 particle, and makes an important interaction with the cellular protein cyclophilin A (CypA). Here, we report crystal structures of the mature CA N-terminal domain (CA(N)(133-278)) and a MA-CA(N) fusion (Gag(1-278)) at resolutions/R(free) values of 1.9 A/25.7% and 2.2 A/25.8%, respectively. Consistent with earlier studies, a comparison of these structures indicates that processing at the MA-CA junction causes CA to adopt an N-terminal beta-hairpin conformation that seems to be required for capsid morphology and viral infectivity. In contrast with an NMR study (Tang, C., et al. (2002) Nat. Struct. Biol. 9, 537-543), structural overlap reveals only small relative displacements for helix 6, which is located between the beta-hairpin and the CypA-binding loop. These observations argue against the proposal that CypA binding is coupled with beta-hairpin formation and support an earlier surface plasmon resonance study (Yoo, S., et al. (1997) J. Mol. Biol. 269, 780-795), which concluded that beta-hairpin formation and CypA-binding are energetically independent events.
About this StructureAbout this Structure
2GOL is a Protein complex structure of sequences from Human immunodeficiency virus 1 with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Implications for viral capsid assembly from crystal structures of HIV-1 Gag(1-278) and CA(N)(133-278)., Kelly BN, Howard BR, Wang H, Robinson H, Sundquist WI, Hill CP, Biochemistry. 2006 Sep 26;45(38):11257-66. PMID:16981686
Page seeded by OCA on Thu Feb 21 17:33:42 2008