Gag polyprotein - Revision history

Alexander Berchansky at 11:50, 29 April 2022

Alexander Berchansky — Fri, 29 Apr 2022 11:50:29 GMT

←Older revision		Revision as of 11:50, 29 April 2022
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	==Capsid (CA) Domain==		==Capsid (CA) Domain==
-	Overall, the mature CA<sup>N</sup> domain is very similar in structure to the corresponding domain of the immature Gag<sup>283</sup> polyprotein ~~<ref name="source" />~~. The CA<sup>N</sup> protein contains 7 α-helices (helix 1-helix 7) that pack together to form a triangular shape, which helps facilitate the final complex formation for the capsid core particles. There are two significant structural differences between the immature and mature versions of the CA<sup>N</sup> domain: an N-terminal β-hairpin and a 2-Angstrom displacement of helix 6.	+	Overall, the mature CA<sup>N</sup> domain is very similar in structure to the corresponding domain of the immature Gag<sup>283</sup> polyprotein. The CA<sup>N</sup> protein contains 7 α-helices (helix 1-helix 7) that pack together to form a triangular shape, which helps facilitate the final complex formation for the capsid core particles. There are two significant structural differences between the immature and mature versions of the CA<sup>N</sup> domain: an N-terminal β-hairpin and a 2-Angstrom displacement of helix 6.

	In the mature CA<sup>N</sup> protein, the N-terminal residues form an anti-parallel β-hairpin instead of the random coil that is observed when the same residues are compared in the immature Gag<sup>283</sup> polyprotein. The NH<sub>2</sub>+ group of the N-terminus proline establishes a salt bridge with a nearby aspartic acid, which stabilizes the β-hairpin. This N-terminal β-hairpin is required for the final formation of the viral capsid, and many studies have shown through conservation and mutagenesis that this β-hairpin is responsible for the stabilization of the protein complexes involved in the capsid formation <ref name="gitti">PMID:8662505</ref><ref name="von">PMID:9501077</ref>.		In the mature CA<sup>N</sup> protein, the N-terminal residues form an anti-parallel β-hairpin instead of the random coil that is observed when the same residues are compared in the immature Gag<sup>283</sup> polyprotein. The NH<sub>2</sub>+ group of the N-terminus proline establishes a salt bridge with a nearby aspartic acid, which stabilizes the β-hairpin. This N-terminal β-hairpin is required for the final formation of the viral capsid, and many studies have shown through conservation and mutagenesis that this β-hairpin is responsible for the stabilization of the protein complexes involved in the capsid formation <ref name="gitti">PMID:8662505</ref><ref name="von">PMID:9501077</ref>.

Michal Harel at 09:09, 8 July 2019

Michal Harel — Mon, 08 Jul 2019 09:09:09 GMT

←Older revision		Revision as of 09:09, 8 July 2019
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	</StructureSection>		</StructureSection>
-	==3D structures of Gag polyprotein==

-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*Gag polyprotein from HIV-1
-
-	**[[2h3i]] – Gag residues 2-132 – HIV-1<BR />
-	**[[2h3f]], [[2h3i]], [[1uph]] - Gag residues 2-132 – NMR<BR />
-	**[[5mdg]], [[5mdf]], [[5mde]], [[5mdd]], [[5mdc]], [[5mdb]], [[5mda]], [[5md9]], [[5md8]], [[5md7]], [[5md6]], [[5md5]], [[5md4]], [[5md3]], [[5md2]], [[5md1]], [[5md0]], [[5mcz]] - Gag residues 1-221 – Cryo EM<br />
-	**[[1l6n]] - Gag residues 1-283 – NMR<BR />
-	**[[1gwp]] - Gag residues 132-283 – NMR<BR />
-	**[[2jmg]], [[2nv3]] - Gag residues 2-132 (mutant) – NMR<BR />
-	**[[1u57]] - Gag residues 1-48 – NMR<BR />
-	**[[1esk]] - Gag residues 12-53 – NMR<BR />
-	**[[1baj]] – Gag C terminal<BR />
-	**[[2znf]] – Gag zinc fingerlike domain - NMR<BR />
-	**[[5teo]] - Gag residues 278-377 <br />
-	**[[6n3j]] - Gag residues 278-377 (mutant) <br />
-	**[[2h3q]], [[2h3v]], [[2h3z]] - Gag residues 2-132 + phosphatidyl inositol bisphosphate - NMR<BR />
-	**[[1mt7]], [[1mt8]] – Gag MA-CA cleavage site + protease retropepsin (mutant) <BR />
-	*[[1agb]], [[1agc]], [[1agd]], [[1age]], [[1agf]] – Gag peptide + β-2 microglobulin + B0801<BR />
-	**[[3p9g]], [[3p9h]], [[3obu]], [[3obx]], [[1m4p]], [[1m4q]] - Gag peptide + tumor susceptibility gene 101 protein N terminal<BR />
-	**[[1fgl]] – Gag residues 81-105 + cyclophilin A<BR />
-	**[[2xde]] - Gag residues 1-146 + inhibitor<BR />
-	**[[4j91]], [[4j92]], [[4j93]] - Gag residues 133-278 + inhibitor<br />
-	**[[6n3u]] - Gag residues 278-377 (mutant) + inhibitor<br />
-	**[[2x2d]] - Gag residues 133-278 + peptidyl-prolyl cis-trans isomerase A<BR />
-	**[[2lf4]] - Gag residues 133-363 (mutant)<br />
-	**[[4u0d]] - Gag residues 133-363 + Nup153 peptide<br />
-	**[[5upw]], [[5mcy]], [[5mcx]] - Gag residues 139-351 – Cryo EM<br />
-	**[[6ern]] - Gag residues 139-351 + ATP<br />
-	**[[6erm]] - Gag residues 139-351 + TTP derivative<br />
-	**[[6h09]], [[6es8]] - Gag residues 133-315 + inositol hexakisphosphate<br />
-	**[[2xt1]] – Gag C terminal + camelid VHH<br />
-	**[[1sje]], [[1sjh]] – Gag peptide + HLA-DR1<BR />
-	**[[1kj4]], [[1kj7]], [[1kjf]], [[1kjg]] - Gag peptide + POL polyprotein
-
-	*Gag polyprotein from HIV-2
-
-	**[[2wlv]] - Gag residues 99-242 – HIV-2<BR />
-	**[[2ec7]] – Gag – NMR<BR />
-
-	*Gag polyprotein from Rous sarcoma virus
-
-	**[[3g0v]], [[3g1g]], [[3g21]], [[3g1i]] - Gag C terminal – Rous sarcoma virus<BR />
-	**[[3g26]], [[3g28]], [[3g29]] - Gag C terminal (mutant) <BR />
-	**[[1p7n]] – Gag N terminal<BR />
-	**[[1em9]] - Gag N terminal – NMR<BR />
-	**[[1eoq]] - Gag C terminal – NMR<BR />
-	**[[1a6s]] – Gag M domain (mutant) - NMR<BR />
-	**[[5a9e]] - Gag residues 84-577 – Cryo EM<br />
-
-	*Gag polyprotein from Simian immunodeficiency virus
-
-	**[[1ecw]], [[1ed1]] - Gag<BR />
-	**[[2xs1]] - Gag peptide + programmed cell death 6-interacting protein
-
-	*Gag polyprotein from Moloney murine leukemia virus
-
-	**[[1u7k]], [[3bp9]] - Gag residues 215-345<BR />
-	**[[1u6p]] – Gag residues 479-534 + DNA <br />
-	**[[6mig]] - Gag residues 683-937 + DNA<br />
-
-	*Gag polyprotein from equine infectious anemia virus
-
-	**[[1hek]] – Gag
-
-	*Gag polyprotein from Mason-Pfizer monkey virus
-
-	**[[1cl4]] - Gag residues 49-80 (mutant) – NMR<BR />
-
-	*Gag polyprotein from human spumaretrovirus
-
-	**[[4jnh]] - Gag N terminal <br />
-	**[[4jmr]] - Gag N terminal + Env protein<br />
-	**[[5m1h]], [[5m1g]] - Gag residues 300-477 - NMR<br />
-	}}
	==Additional Resources==		==Additional Resources==
	For additional information, see: [[Human Immunodeficiency Virus]]		For additional information, see: [[Human Immunodeficiency Virus]]

Michal Harel at 09:04, 8 July 2019

Michal Harel — Mon, 08 Jul 2019 09:04:56 GMT

←Older revision		Revision as of 09:04, 8 July 2019
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	<StructureSection load='2wlv' size='350' side='right' caption='Gag polyprotein N-terminal capsid domain of HIV-2 (PDB entry [[2wlv]])' scene=''>		<StructureSection load='2wlv' size='350' side='right' caption='Gag polyprotein N-terminal capsid domain of HIV-2 (PDB entry [[2wlv]])' scene=''>

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	==Implications==		==Implications==
	HIV-1 viral particles need to form a capsid cone-like structure prior to infection of the host cell. The protealytic cleavage of the immature Gag<sup>283</sup> polyprotein results in a capsid domain. This post-translational modification is essential to the formation of the core structure. Many studies have shown that the β-hairpin formed after maturation is essential for the capsid core particle formation <ref name="gitti"/><ref name="von"/>. As a result of the β-hairpin formation, the helix 6 is displaced causing an allosteric mechanism for CpyA binding. Overall, the maturation of Gag<sup>283</sup> and formation of the mature CA protein is essential for core capsid particle creation and consequently final infection.		HIV-1 viral particles need to form a capsid cone-like structure prior to infection of the host cell. The protealytic cleavage of the immature Gag<sup>283</sup> polyprotein results in a capsid domain. This post-translational modification is essential to the formation of the core structure. Many studies have shown that the β-hairpin formed after maturation is essential for the capsid core particle formation <ref name="gitti"/><ref name="von"/>. As a result of the β-hairpin formation, the helix 6 is displaced causing an allosteric mechanism for CpyA binding. Overall, the maturation of Gag<sup>283</sup> and formation of the mature CA protein is essential for core capsid particle creation and consequently final infection.
		+
		+	==3D structures of Gag polyprotein==
		+	[[Gag polyprotein 3D structures]]
		+
	</StructureSection>		</StructureSection>
	==3D structures of Gag polyprotein==		==3D structures of Gag polyprotein==
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	**[[2h3i]] – Gag residues 2-132 – HIV-1<BR />		**[[2h3i]] – Gag residues 2-132 – HIV-1<BR />
	**[[2h3f]], [[2h3i]], [[1uph]] - Gag residues 2-132 – NMR<BR />		**[[2h3f]], [[2h3i]], [[1uph]] - Gag residues 2-132 – NMR<BR />
		+	**[[5mdg]], [[5mdf]], [[5mde]], [[5mdd]], [[5mdc]], [[5mdb]], [[5mda]], [[5md9]], [[5md8]], [[5md7]], [[5md6]], [[5md5]], [[5md4]], [[5md3]], [[5md2]], [[5md1]], [[5md0]], [[5mcz]] - Gag residues 1-221 – Cryo EM<br />
	**[[1l6n]] - Gag residues 1-283 – NMR<BR />		**[[1l6n]] - Gag residues 1-283 – NMR<BR />
	**[[1gwp]] - Gag residues 132-283 – NMR<BR />		**[[1gwp]] - Gag residues 132-283 – NMR<BR />
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	**[[1baj]] – Gag C terminal<BR />		**[[1baj]] – Gag C terminal<BR />
	**[[2znf]] – Gag zinc fingerlike domain - NMR<BR />		**[[2znf]] – Gag zinc fingerlike domain - NMR<BR />
		+	**[[5teo]] - Gag residues 278-377 <br />
		+	**[[6n3j]] - Gag residues 278-377 (mutant) <br />
	**[[2h3q]], [[2h3v]], [[2h3z]] - Gag residues 2-132 + phosphatidyl inositol bisphosphate - NMR<BR />		**[[2h3q]], [[2h3v]], [[2h3z]] - Gag residues 2-132 + phosphatidyl inositol bisphosphate - NMR<BR />
	**[[1mt7]], [[1mt8]] – Gag MA-CA cleavage site + protease retropepsin (mutant) <BR />		**[[1mt7]], [[1mt8]] – Gag MA-CA cleavage site + protease retropepsin (mutant) <BR />
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	**[[1fgl]] – Gag residues 81-105 + cyclophilin A<BR />		**[[1fgl]] – Gag residues 81-105 + cyclophilin A<BR />
	**[[2xde]] - Gag residues 1-146 + inhibitor<BR />		**[[2xde]] - Gag residues 1-146 + inhibitor<BR />
-	**[[~~4e91~~]], [[~~4e92~~]] - Gag residues 133-278 + inhibitor<br />	+	**[[4j91]], [[4j92]], [[4j93]] - Gag residues 133-278 + inhibitor<br />
		+	**[[6n3u]] - Gag residues 278-377 (mutant) + inhibitor<br />
	**[[2x2d]] - Gag residues 133-278 + peptidyl-prolyl cis-trans isomerase A<BR />		**[[2x2d]] - Gag residues 133-278 + peptidyl-prolyl cis-trans isomerase A<BR />
	**[[2lf4]] - Gag residues 133-363 (mutant)<br />		**[[2lf4]] - Gag residues 133-363 (mutant)<br />
		+	**[[4u0d]] - Gag residues 133-363 + Nup153 peptide<br />
		+	**[[5upw]], [[5mcy]], [[5mcx]] - Gag residues 139-351 – Cryo EM<br />
		+	**[[6ern]] - Gag residues 139-351 + ATP<br />
		+	**[[6erm]] - Gag residues 139-351 + TTP derivative<br />
		+	**[[6h09]], [[6es8]] - Gag residues 133-315 + inositol hexakisphosphate<br />
	**[[2xt1]] – Gag C terminal + camelid VHH<br />		**[[2xt1]] – Gag C terminal + camelid VHH<br />
	**[[1sje]], [[1sjh]] – Gag peptide + HLA-DR1<BR />		**[[1sje]], [[1sjh]] – Gag peptide + HLA-DR1<BR />
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	**[[1eoq]] - Gag C terminal – NMR<BR />		**[[1eoq]] - Gag C terminal – NMR<BR />
	**[[1a6s]] – Gag M domain (mutant) - NMR<BR />		**[[1a6s]] – Gag M domain (mutant) - NMR<BR />
		+	**[[5a9e]] - Gag residues 84-577 – Cryo EM<br />

	*Gag polyprotein from Simian immunodeficiency virus		*Gag polyprotein from Simian immunodeficiency virus
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	**[[1u7k]], [[3bp9]] - Gag residues 215-345<BR />		**[[1u7k]], [[3bp9]] - Gag residues 215-345<BR />
-	**[[1u6p]] – Gag ~~fragment~~ + DNA ~~– Moloney murine leukemia virus~~	+	**[[1u6p]] – Gag residues 479-534 + DNA <br />
		+	**[[6mig]] - Gag residues 683-937 + DNA<br />

	*Gag polyprotein from equine infectious anemia virus		*Gag polyprotein from equine infectious anemia virus
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	**[[4jnh]] - Gag N terminal <br />		**[[4jnh]] - Gag N terminal <br />
		+	**[[4jmr]] - Gag N terminal + Env protein<br />
		+	**[[5m1h]], [[5m1g]] - Gag residues 300-477 - NMR<br />
	}}		}}
	==Additional Resources==		==Additional Resources==

Joel L. Sussman at 11:17, 20 October 2017

Joel L. Sussman — Fri, 20 Oct 2017 11:17:10 GMT

←Older revision		Revision as of 11:17, 20 October 2017
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	<StructureSection load='2wlv' size='350' side='right' caption='Gag polyprotein N-terminal capsid domain of HIV-2 (PDB entry [[2wlv]])' scene=''>		<StructureSection load='2wlv' size='350' side='right' caption='Gag polyprotein N-terminal capsid domain of HIV-2 (PDB entry [[2wlv]])' scene=''>
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	== Function ==		== Function ==

Michal Harel at 19:19, 19 October 2017

Michal Harel — Thu, 19 Oct 2017 19:19:46 GMT

←Older revision		Revision as of 19:19, 19 October 2017
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-		+	<StructureSection load='2wlv' size='350' side='right' caption='Gag polyprotein N-terminal capsid domain of HIV-2 (PDB entry [[2wlv]])' scene=''>
-	<StructureSection load='2wlv' size='~~450~~' side='right' caption='Gag polyprotein N-terminal capsid domain of HIV-2 (PDB entry [[2wlv]])' scene=''>	+

Michal Harel at 19:19, 19 October 2017

Michal Harel — Thu, 19 Oct 2017 19:19:17 GMT

←Older revision		Revision as of 19:19, 19 October 2017
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-	[[Image:1gwp.png\|left\|200px\|thumb\|The mature CA<sup>N</sup> domain of the [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_12) HIV-1] Gag<sup>283</sup> polyprotein ([[1gwp]]), is a protein involved in formation of the capsid core particle. The structure of the CA<sup>N</sup> domain was determined through [[NMR]] by Tang et al. <ref name="source">PMID:12032547</ref>.]]	+

Michal Harel at 10:28, 22 May 2017

Michal Harel — Mon, 22 May 2017 10:28:40 GMT

←Older revision		Revision as of 10:28, 22 May 2017
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	[[Image:1gwp.png\|left\|200px\|thumb\|The mature CA<sup>N</sup> domain of the [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_12) HIV-1] Gag<sup>283</sup> polyprotein ([[1gwp]]), is a protein involved in formation of the capsid core particle. The structure of the CA<sup>N</sup> domain was determined through [[NMR]] by Tang et al. <ref name="source">PMID:12032547</ref>.]]		[[Image:1gwp.png\|left\|200px\|thumb\|The mature CA<sup>N</sup> domain of the [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_12) HIV-1] Gag<sup>283</sup> polyprotein ([[1gwp]]), is a protein involved in formation of the capsid core particle. The structure of the CA<sup>N</sup> domain was determined through [[NMR]] by Tang et al. <ref name="source">PMID:12032547</ref>.]]

-	~~{{STRUCTURE_2wlv\| PDB~~=2wlv ~~\| SIZE~~=~~400\| SCENE~~= \|right~~\|CAPTION~~=Gag polyprotein N-terminal capsid domain of HIV-2, [[2wlv]] }}	+
		+	<StructureSection load='2wlv' size='450' side='right' caption='Gag polyprotein N-terminal capsid domain of HIV-2 (PDB entry [[2wlv]])' scene=''>


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	==Implications==		==Implications==
	HIV-1 viral particles need to form a capsid cone-like structure prior to infection of the host cell. The protealytic cleavage of the immature Gag<sup>283</sup> polyprotein results in a capsid domain. This post-translational modification is essential to the formation of the core structure. Many studies have shown that the β-hairpin formed after maturation is essential for the capsid core particle formation <ref name="gitti"/><ref name="von"/>. As a result of the β-hairpin formation, the helix 6 is displaced causing an allosteric mechanism for CpyA binding. Overall, the maturation of Gag<sup>283</sup> and formation of the mature CA protein is essential for core capsid particle creation and consequently final infection.		HIV-1 viral particles need to form a capsid cone-like structure prior to infection of the host cell. The protealytic cleavage of the immature Gag<sup>283</sup> polyprotein results in a capsid domain. This post-translational modification is essential to the formation of the core structure. Many studies have shown that the β-hairpin formed after maturation is essential for the capsid core particle formation <ref name="gitti"/><ref name="von"/>. As a result of the β-hairpin formation, the helix 6 is displaced causing an allosteric mechanism for CpyA binding. Overall, the maturation of Gag<sup>283</sup> and formation of the mature CA protein is essential for core capsid particle creation and consequently final infection.
-		+	</StructureSection>
	==3D structures of Gag polyprotein==		==3D structures of Gag polyprotein==

Michal Harel at 07:39, 3 March 2016

Michal Harel — Thu, 03 Mar 2016 07:39:02 GMT

←Older revision		Revision as of 07:39, 3 March 2016
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		+	== Function ==

	The '''Gag polyprotein''' (Gag) is part of the basic infrastructure of retroviruses. The Gag is processed during maturation to '''matrix protein (MA)''', '''capsid protein (CA)''', '''spacer peptides (SP1, SP2)''', '''nucleocapsid protein (NC)''' and '''p6'''. For detailed discussion of HIV-1 Gag polyprotein see [[Hiv-1 gag]].		The '''Gag polyprotein''' (Gag) is part of the basic infrastructure of retroviruses. The Gag is processed during maturation to '''matrix protein (MA)''', '''capsid protein (CA)''', '''spacer peptides (SP1, SP2)''', '''nucleocapsid protein (NC)''' and '''p6'''. For detailed discussion of HIV-1 Gag polyprotein see [[Hiv-1 gag]].

Michal Harel at 12:56, 25 November 2014

Michal Harel — Tue, 25 Nov 2014 12:56:45 GMT

Michal Harel at 09:33, 27 July 2014

Michal Harel — Sun, 27 Jul 2014 09:33:16 GMT

←Older revision		Revision as of 09:33, 27 July 2014
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-	The '''Gag polyprotein''' (Gag) is part of the basic infrastructure of retroviruses. The Gag is processed during maturation of matrix protein, capsid protein, spacer ~~peptide and~~ nucleocapsid protein. For detailed discussion of HIV-1 Gag polyprotein see [[Hiv-1 gag]].	+	The '''Gag polyprotein''' (Gag) is part of the basic infrastructure of retroviruses. The Gag is processed during maturation to '''matrix protein (MA)''', '''capsid protein (CA)''', '''spacer peptides (SP1, SP2)''', '''nucleocapsid protein (NC)''' and '''p6'''. For detailed discussion of HIV-1 Gag polyprotein see [[Hiv-1 gag]].

	Gag of [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_12) human immunodeficiency virus type 1] (HIV-1), is a primary protein involved in the packaging of two copies of the viral genome for capsid formation <ref>Coffin, J., S. Hughes, and H. Varmus, Retroviruses. 1997: Cold Spring Harbor Laboratory Press.</ref>. In the cytoplasm of the infected cell, Gag is translated and approximately 1500 copies of the immature HIV-1 Gag polyprotein [[1l6n]] come together to form an immature viral particle. After budding of the viral particle, viral proteases cleave the Gag protein into three structurally different products: the matrix, the capsid, and the nucleocapsid. The protealytic cleavage results in viral maturation and induces significant structural changes of the protein products. Following this proteolysis, the viral particle takes on the classic cone shape required for a new infection.		Gag of [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_12) human immunodeficiency virus type 1] (HIV-1), is a primary protein involved in the packaging of two copies of the viral genome for capsid formation <ref>Coffin, J., S. Hughes, and H. Varmus, Retroviruses. 1997: Cold Spring Harbor Laboratory Press.</ref>. In the cytoplasm of the infected cell, Gag is translated and approximately 1500 copies of the immature HIV-1 Gag polyprotein [[1l6n]] come together to form an immature viral particle. After budding of the viral particle, viral proteases cleave the Gag protein into three structurally different products: the matrix, the capsid, and the nucleocapsid. The protealytic cleavage results in viral maturation and induces significant structural changes of the protein products. Following this proteolysis, the viral particle takes on the classic cone shape required for a new infection.

←Older revision		Revision as of 12:56, 25 November 2014
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	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}		Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
		+	{{#tree:id=OrganizedByTopic\|openlevels=0\|

-	~~===~~Gag polyprotein from HIV-1~~===~~	+	*Gag polyprotein from HIV-1

-	[[2h3i]] – Gag residues 2-132 – HIV-1<BR />	+	**[[2h3i]] – Gag residues 2-132 – HIV-1<BR />
-	[[2h3f]], [[2h3i]], [[1uph]] - Gag residues 2-132 – NMR<BR />	+	**[[2h3f]], [[2h3i]], [[1uph]] - Gag residues 2-132 – NMR<BR />
-	[[1l6n]] - Gag residues 1-283 – NMR<BR />	+	**[[1l6n]] - Gag residues 1-283 – NMR<BR />
-	[[1gwp]] - Gag residues 132-283 – NMR<BR />	+	**[[1gwp]] - Gag residues 132-283 – NMR<BR />
-	[[2jmg]], [[2nv3]] - Gag residues 2-132 (mutant) – NMR<BR />	+	**[[2jmg]], [[2nv3]] - Gag residues 2-132 (mutant) – NMR<BR />
-	[[1u57]] - Gag residues 1-48 – NMR<BR />	+	**[[1u57]] - Gag residues 1-48 – NMR<BR />
-	[[1esk]] - Gag residues 12-53 – NMR<BR />	+	**[[1esk]] - Gag residues 12-53 – NMR<BR />
-	[[1baj]] – Gag C terminal<BR />	+	**[[1baj]] – Gag C terminal<BR />
-	[[2znf]] – Gag zinc fingerlike domain - NMR<BR />	+	**[[2znf]] – Gag zinc fingerlike domain - NMR<BR />
-	[[2h3q]], [[2h3v]], [[2h3z]] - Gag residues 2-132 + phosphatidyl inositol bisphosphate - NMR<BR />	+	**[[2h3q]], [[2h3v]], [[2h3z]] - Gag residues 2-132 + phosphatidyl inositol bisphosphate - NMR<BR />
-	[[1mt7]], [[1mt8]] – Gag MA-CA cleavage site + protease retropepsin (mutant) <BR />	+	**[[1mt7]], [[1mt8]] – Gag MA-CA cleavage site + protease retropepsin (mutant) <BR />
-	[[1agb]], [[1agc]], [[1agd]], [[1age]], [[1agf]] – Gag peptide + β-2 microglobulin + B*0801<BR />	+	*[[1agb]], [[1agc]], [[1agd]], [[1age]], [[1agf]] – Gag peptide + β-2 microglobulin + B0801<BR />
-	[[3p9g]], [[3p9h]], [[3obu]], [[3obx]], [[1m4p]], [[1m4q]] - Gag peptide + tumor susceptibility gene 101 protein N terminal<BR />	+	**[[3p9g]], [[3p9h]], [[3obu]], [[3obx]], [[1m4p]], [[1m4q]] - Gag peptide + tumor susceptibility gene 101 protein N terminal<BR />
-	[[1fgl]] – Gag residues 81-105 + cyclophilin A<BR />	+	**[[1fgl]] – Gag residues 81-105 + cyclophilin A<BR />
-	[[2xde]] - Gag residues 1-146 + inhibitor<BR />	+	**[[2xde]] - Gag residues 1-146 + inhibitor<BR />
-	[[4e91]], [[4e92]] - Gag residues 133-278 + inhibitor<br />	+	**[[4e91]], [[4e92]] - Gag residues 133-278 + inhibitor<br />
-	[[2x2d]] - Gag residues 133-278 + peptidyl-prolyl cis-trans isomerase A<BR />	+	**[[2x2d]] - Gag residues 133-278 + peptidyl-prolyl cis-trans isomerase A<BR />
-	[[2lf4]] - Gag residues 133-363 (mutant)<br />	+	**[[2lf4]] - Gag residues 133-363 (mutant)<br />
-	[[2xt1]] – Gag C terminal + camelid VHH<br />	+	**[[2xt1]] – Gag C terminal + camelid VHH<br />
-	[[1sje]], [[1sjh]] – Gag peptide + HLA-DR1<BR />	+	**[[1sje]], [[1sjh]] – Gag peptide + HLA-DR1<BR />
-	[[1kj4]], [[1kj7]], [[1kjf]], [[1kjg]] - Gag peptide + POL polyprotein	+	**[[1kj4]], [[1kj7]], [[1kjf]], [[1kjg]] - Gag peptide + POL polyprotein

-	~~===~~Gag polyprotein from HIV-2~~===~~	+	*Gag polyprotein from HIV-2

-	[[2wlv]] - Gag residues 99-242 – HIV-2<BR />	+	**[[2wlv]] - Gag residues 99-242 – HIV-2<BR />
-	[[2ec7]] – Gag – NMR<BR />	+	**[[2ec7]] – Gag – NMR<BR />

-	~~===~~Gag polyprotein from Rous sarcoma virus~~===~~	+	*Gag polyprotein from Rous sarcoma virus

-	[[3g0v]], [[3g1g]], [[3g21]], [[3g1i]] - Gag C terminal – Rous sarcoma virus<BR />	+	**[[3g0v]], [[3g1g]], [[3g21]], [[3g1i]] - Gag C terminal – Rous sarcoma virus<BR />
-	[[3g26]], [[3g28]], [[3g29]] - Gag C terminal (mutant) <BR />	+	**[[3g26]], [[3g28]], [[3g29]] - Gag C terminal (mutant) <BR />
-	[[1p7n]] – Gag N terminal<BR />	+	**[[1p7n]] – Gag N terminal<BR />
-	[[1em9]] - Gag N terminal – NMR<BR />	+	**[[1em9]] - Gag N terminal – NMR<BR />
-	[[1eoq]] - Gag C terminal – NMR<BR />	+	**[[1eoq]] - Gag C terminal – NMR<BR />
-	[[1a6s]] – Gag M domain (mutant) - NMR<BR />	+	**[[1a6s]] – Gag M domain (mutant) - NMR<BR />

-	~~===~~Gag polyprotein from Simian immunodeficiency virus~~===~~	+	*Gag polyprotein from Simian immunodeficiency virus

-	[[1ecw]], [[1ed1]] - Gag<BR />	+	**[[1ecw]], [[1ed1]] - Gag<BR />
-	[[2xs1]] - Gag peptide + programmed cell death 6-interacting protein	+	**[[2xs1]] - Gag peptide + programmed cell death 6-interacting protein

-	~~===~~Gag polyprotein from Moloney murine leukemia virus~~===~~	+	*Gag polyprotein from Moloney murine leukemia virus

-	[[1u7k]], [[3bp9]] - Gag residues 215-345<BR />	+	**[[1u7k]], [[3bp9]] - Gag residues 215-345<BR />
-	[[1u6p]] – Gag fragment + DNA – Moloney murine leukemia virus	+	**[[1u6p]] – Gag fragment + DNA – Moloney murine leukemia virus

-	~~===~~Gag polyprotein from equine infectious anemia virus~~===~~	+	*Gag polyprotein from equine infectious anemia virus

-	[[1hek]] – Gag	+	**[[1hek]] – Gag

-	~~===~~Gag polyprotein from Mason-Pfizer monkey virus~~===~~	+	*Gag polyprotein from Mason-Pfizer monkey virus

-	[[1cl4]] - Gag residues 49-80 (mutant) – NMR<BR />	+	**[[1cl4]] - Gag residues 49-80 (mutant) – NMR<BR />

-	~~===~~Gag polyprotein from human spumaretrovirus~~===~~	+	*Gag polyprotein from human spumaretrovirus
-		+
-	~~[[4jnh]] - Gag N terminal <br />~~	+

		+	**[[4jnh]] - Gag N terminal <br />
		+	}}
	==Additional Resources==		==Additional Resources==
	For additional information, see: [[Human Immunodeficiency Virus]]		For additional information, see: [[Human Immunodeficiency Virus]]