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InterPro: IPR000721 Retroviral nucleocapsid protein Gag

Protein matches Help

UniProtKB

Matches:

26481 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000721 Gag_p24

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00607	Gag_p24	26481
Signatures in BioMart

InterPro Relationships Help

Contains

IPR008916 Retrovirus capsid, C-terminal
IPR008919 Retrovirus capsid, N-terminal core

GO Term annotation Help

Process

GO:0016032 viral reproduction

InterPro annotation

Entry Details in BioMart

Abstract

The Gag protein from retroviruses, also known as p24, forms the inner protein layer of the nucleocapsid. This protein performs highly complex orchestrated tasks during the assembly, budding, maturation and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.

Structural links Help

PDB - click here

SCOP: a.28.3.1 , a.73.1.1 , j.47.1.1

CATH: 1.10.1200.30 , 1.10.375.10 , 1.20.5.760

Database links Help

PANDIT: PF00607

Blocks: IPB000721

Pfam Clan: CL0148.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000721

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O12158 Gag-Pol polyprotein

P03975 IgE-binding protein

P62683 HERV-K_12q14.1 provirus ancestral Gag polyprotein

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003308	Integrase, N-terminal zinc-binding domain
IPR012337	Polynucleotidyl transferase, ribonuclease H fold
IPR008919	Retrovirus capsid, N-terminal core
IPR008916	Retrovirus capsid, C-terminal
IPR002156	Ribonuclease H
IPR018061	Peptidase A2A, retrovirus RVP subgroup
IPR001878	Zinc finger, CCHC-type
IPR017856	Integrase, N-terminal zinc-binding domain-like
IPR009007	Peptidase aspartic, catalytic
IPR001969	Peptidase aspartic, active site
IPR003322	Beta-retroviral matrix, N-terminal
IPR010659	Reverse transcriptase connection
IPR010999	Retroviral matrix, N-terminal
IPR010661	Reverse transcriptase thumb
IPR000477	RNA-directed DNA polymerase (reverse transcriptase)
IPR013084	Zinc finger, CCHC retroviral-type
IPR000721	Retroviral nucleocapsid protein Gag
IPR000071	Immunodeficiency lentiviral matrix, N-terminal
IPR012344	Matrix protein, N-terminal, lentiviral and alpha-retroviral
IPR001584	Integrase, catalytic core
IPR001995	Peptidase A2A, retrovirus, catalytic
IPR001037	Integrase, C-terminal, retroviral
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Ternois F, Sticht J, Duquerroy S, Krausslich HG, Rey FA. The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor. Nat. Struct. Mol. Biol. 12 2005 678-82 [PubMed: 16041386] http://dx.doi.org/10.1038/nsmb967
	Sticht J, Humbert M, Findlow S, Bodem J, Muller B, Dietrich U, Werner J, Krausslich HG. A peptide inhibitor of HIV-1 assembly in vitro. Nat. Struct. Mol. Biol. 12 2005 671-7 [PubMed: 16041387] http://dx.doi.org/10.1038/nsmb964
	Wehrly K, Chesebro B. p24 antigen capture assay for quantification of human immunodeficiency virus using readily available inexpensive reagents. Methods 12 1997 288-93 [PubMed: 9245608] http://dx.doi.org/10.1006/meth.1997.0481
	Kelly BN, Kyere S, Kinde I, Tang C, Howard BR, Robinson H, Sundquist WI, Summers MF, Hill CP. Structure of the antiviral assembly inhibitor CAP-1 complex with the HIV-1 CA protein. J. Mol. Biol. 373 2007 355-66 [PubMed: 17826792] http://dx.doi.org/10.1016/j.jmb.2007.07.070
	Kelly BN, Howard BR, Wang H, Robinson H, Sundquist WI, Hill CP. Implications for viral capsid assembly from crystal structures of HIV-1 Gag(1-278) and CA(N)(133-278). Biochemistry 45 2006 11257-66 [PubMed: 16981686] http://dx.doi.org/10.1021/bi060927x
	Morellet N, Druillennec S, Lenoir C, Bouaziz S, Roques BP. Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging. Protein Sci. 14 2005 375-86 [PubMed: 15659370] http://dx.doi.org/10.1110/ps.041087605

InterPro 23.1