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InterPro: IPR008919 Retrovirus capsid, N-terminal core

Protein matchesHelp
UniProtKB
Matches:
25991 proteins
AccessionHelp IPR008919 Retrov_capsid_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR000721 Retroviral nucleocapsid protein Gag
GO Term annotationHelp
Process GO:0016032 viral reproduction
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The Gag polyprotein from retroviruses is processed by viral protease to produce the major structural proteins, including the capsid protein. The newly formed capsid protein rearranges to form the capsid core particle that surrounds the viral genome of the mature virus. The capsid is composed of two domains, the N-terminal domain (NTD), which contributes to viral core formation, and the C-terminal domain (CTD), which is required for capsid dimerisation, Gag oligomerization and viral formation. The NTD is composed of a five-helix bundle [1, 2].

Structural linksHelp

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008919 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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

PublicationsHelp
1. Jin Z, Jin L, Peterson DL, Lawson CL.
Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26.
J. Mol. Biol. 286 83-93 1999 [PubMed: 9931251]
http://dx.doi.org/10.1006/jmbi.1998.2443
2. Campos-Olivas R, Newman JL, Summers MF.
Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses.
J. Mol. Biol. 296 633-49 2000 [PubMed: 10669613]
http://dx.doi.org/10.1006/jmbi.1999.3475

Additional ReadingHelp
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
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
Saad JS, Miller J, Tai J, Kim A, Ghanam RH, Summers MF.
Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 11364-9 [PubMed: 16840558]
http://dx.doi.org/10.1073/pnas.0602818103
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
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InterPro 23.1