PDBsum entry 1ak4

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protein Protein-protein interface(s) links
Viral protein/isomerase PDB id
Protein chains
165 a.a. *
145 a.a. *
Waters ×321
* Residue conservation analysis
PDB id:
Name: Viral protein/isomerase
Title: Human cyclophilin a bound to the amino-terminal domain of HIV-1 capsid
Structure: Cyclophilin a. Chain: a, b. Engineered: yes. HIV-1 capsid. Chain: c, d. Fragment: n-terminal domain. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Gene: cyclophilin. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Human immunodeficiency virus 1. Organism_taxid: 11676.
Biol. unit: Monomer (from PDB file)
2.36Å     R-factor:   0.238     R-free:   0.306
Authors: C.P.Hill,T.R.Gamble,F.F.Vajdos,D.K.Worthylake,W.I.Sundquist
Key ref:
T.R.Gamble et al. (1996). Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell, 87, 1285-1294. PubMed id: 8980234 DOI: 10.1016/S0092-8674(00)81823-1
28-May-97     Release date:   15-Oct-97    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P62937  (PPIA_HUMAN) -  Peptidyl-prolyl cis-trans isomerase A
165 a.a.
165 a.a.
Protein chains
Pfam   ArchSchema ?
P12497  (POL_HV1N5) -  Gag-Pol polyprotein
1435 a.a.
145 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: Chains A, B: E.C.  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
   Enzyme class 2: Chains C, D: E.C.  - RNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Deoxynucleoside triphosphate
+ DNA(n)
= diphosphate
+ DNA(n+1)
   Enzyme class 3: Chains C, D: E.C.  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Deoxynucleoside triphosphate
+ DNA(n)
= diphosphate
+ DNA(n+1)
   Enzyme class 4: Chains C, D: E.C.  - Exoribonuclease H.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Exonucleolytic cleavage to 5'-phosphomonoester oligonucleotides in both 5'- to 3'- and 3'- to 5'-directions.
   Enzyme class 5: Chains C, D: E.C.  - Retroviral ribonuclease H.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 6: Chains C, D: E.C.  - HIV-1 retropepsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   8 terms 
  Biological process     viral reproduction   18 terms 
  Biochemical function     protein binding     7 terms  


DOI no: 10.1016/S0092-8674(00)81823-1 Cell 87:1285-1294 (1996)
PubMed id: 8980234  
Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid.
T.R.Gamble, F.F.Vajdos, S.Yoo, D.K.Worthylake, M.Houseweart, W.I.Sundquist, C.P.Hill.
The HIV-1 capsid protein forms the conical core structure at the center of the mature virion. Capsid also binds the human peptidyl prolyl isomerase, cyclophilin A, thereby packaging the enzyme into the virion. Cyclophilin A subsequently performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection. We report the 2.36 A crystal structure of the N-terminal domain of HIV-1 capsid (residues 1-151) in complex with human cyclophilin A. A single exposed capsid loop (residues 85-93) binds in the enzyme's active site, and Pro-90 adopts an unprecedented trans conformation. The structure suggests how cyclophilin A can act as a sequence-specific binding protein and a nonspecific prolyl isomerase. In the crystal lattice, capsid molecules assemble into continuous planar strips. Side by side association of these strips may allow capsid to form the surface of the viral core. Cyclophilin A could then function by weakening the association between capsid strips, thereby promoting disassembly of the viral core.
  Selected figure(s)  
Figure 2.
Figure 2. Interaction between CA[151] and CypA(A) Ribbon diagram of the CA[151]/CypA complex: orientation of CA[151] is similar to that of (1B), and the same color code is used. CypA β strands are shown in red and helices are in green.(B) Tube representation of the CA[151]/CypA complex: orientation is perpendicular to (1B). Both complexes in the asymmetric unit are shown following superposition on the two CypA molecules. Complex 1 is shown in cyan (CA[151]-1) and green (CypA-1), and complex 2 is in magenta (CA[151]-2) and red (CypA-2). Figure 2, Figure 4, and 5 were prepared with MIDASPLUS ( [16]).
Figure 3.
Figure 3. Molecular Recognition between CA[151] and CypASchematic representation of the CA[151] and CypA interface ([55]). Hydrogen bonding interactions are shown when the acceptor-to-donor distance is 3.4 Å or less in one of the two complexes. Van der Waals interactions are defined as contacts of 4.1 Å or less in one of the two complexes.
  The above figures are reprinted by permission from Cell Press: Cell (1996, 87, 1285-1294) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22421880 A.Engelman, and P.Cherepanov (2012).
The structural biology of HIV-1: mechanistic and therapeutic insights.
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22407016 M.E.Caines, K.Bichel, A.J.Price, W.A.McEwan, G.J.Towers, B.J.Willett, S.M.Freund, and L.C.James (2012).
Diverse HIV viruses are targeted by a conformationally dynamic antiviral.
  Nat Struct Mol Biol, 19, 411-416.
PDB codes: 4dga 4dgb 4dgc 4dgd 4dge
21187419 B.K.Ganser-Pornillos, V.Chandrasekaran, O.Pornillos, J.G.Sodroski, W.I.Sundquist, and M.Yeager (2011).
Hexagonal assembly of a restricting TRIM5alpha protein.
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20602248 A.Galat, and J.Bua (2010).
Molecular aspects of cyclophilins mediating therapeutic actions of their ligands.
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TRIM5 suppresses cross-species transmission of a primate immunodeficiency virus and selects for emergence of resistant variants in the new species.
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20095046 B.Chen, and R.Tycko (2010).
Structural and dynamical characterization of tubular HIV-1 capsid protein assemblies by solid state nuclear magnetic resonance and electron microscopy.
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19910057 B.G.Luttge, and E.O.Freed (2010).
FIV Gag: virus assembly and host-cell interactions.
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19782103 C.S.Adamson, and E.O.Freed (2010).
Novel approaches to inhibiting HIV-1 replication.
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20808866 L.M.Ylinen, A.J.Price, J.Rasaiyaah, S.Hué, N.J.Rose, F.Marzetta, L.C.James, and G.J.Towers (2010).
Conformational adaptation of Asian macaque TRIMCyp directs lineage specific antiviral activity.
  PLoS Pathog, 6, 0.
PDB codes: 2x82 2x83
20364129 M.Lammers, H.Neumann, J.W.Chin, and L.C.James (2010).
Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization.
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PDB codes: 2x25 2x2a 2x2c 2x2d
20219923 M.S.Briones, C.W.Dobard, and S.A.Chow (2010).
Role of human immunodeficiency virus type 1 integrase in uncoating of the viral core.
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A new functional role of HIV-1 integrase during uncoating of the viral core.
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20920334 S.M.Solbak, T.R.Reksten, V.Wray, K.Bruns, O.Horvli, A.J.Raae, P.Henklein, P.Henklein, R.Röder, D.Mitzner, U.Schubert, and T.Fossen (2010).
The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.
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20529865 S.Misumi, M.Inoue, T.Dochi, N.Kishimoto, N.Hasegawa, N.Takamune, and S.Shoji (2010).
Uncoating of human immunodeficiency virus type 1 requires prolyl isomerase Pin1.
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21170360 W.S.Blair, C.Pickford, S.L.Irving, D.G.Brown, M.Anderson, R.Bazin, J.Cao, G.Ciaramella, J.Isaacson, L.Jackson, R.Hunt, A.Kjerrstrom, J.A.Nieman, A.K.Patick, M.Perros, A.D.Scott, K.Whitby, H.Wu, and S.L.Butler (2010).
HIV capsid is a tractable target for small molecule therapeutic intervention.
  PLoS Pathog, 6, e1001220.
PDB code: 2xde
20089655 X.Tian, C.Zhao, H.Zhu, W.She, J.Zhang, J.Liu, L.Li, S.Zheng, Y.M.Wen, and Y.Xie (2010).
Hepatitis B virus (HBV) surface antigen interacts with and promotes cyclophilin a secretion: possible link to pathogenesis of HBV infection.
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20092249 Y.Han, J.Ahn, J.Concel, I.J.Byeon, A.M.Gronenborn, J.Yang, and T.Polenova (2010).
Solid-state NMR studies of HIV-1 capsid protein assemblies.
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19767750 A.J.Price, F.Marzetta, M.Lammers, L.M.Ylinen, T.Schaller, S.J.Wilson, G.J.Towers, and L.C.James (2009).
Active site remodeling switches HIV specificity of antiretroviral TRIMCyp.
  Nat Struct Mol Biol, 16, 1036-1042.
PDB codes: 2wlv 2wlw
19680534 A.Kaul, S.Stauffer, C.Berger, T.Pertel, J.Schmitt, S.Kallis, M.Z.Lopez, V.Lohmann, J.Luban, and R.Bartenschlager (2009).
Essential role of cyclophilin A for hepatitis C virus replication and virus production and possible link to polyprotein cleavage kinetics.
  PLoS Pathog, 5, e1000546.  
19825046 A.P.Mascarenhas, and K.Musier-Forsyth (2009).
The capsid protein of human immunodeficiency virus: interactions of HIV-1 capsid with host protein factors.
  FEBS J, 276, 6118-6127.  
19534569 C.S.Adamson, K.Salzwedel, and E.O.Freed (2009).
Virus maturation as a new HIV-1 therapeutic target.
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19128175 D.Hamelberg, and J.A.McCammon (2009).
Mechanistic insight into the role of transition-state stabilization in cyclophilin A.
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19356593 E.Barklis, A.Alfadhli, C.McQuaw, S.Yalamuri, A.Still, R.L.Barklis, B.Kukull, and C.S.López (2009).
Characterization of the in vitro HIV-1 capsid assembly pathway.
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19478882 F.D.Bushman, N.Malani, J.Fernandes, I.D'Orso, G.Cagney, T.L.Diamond, H.Zhou, D.J.Hazuda, A.S.Espeseth, R.König, S.Bandyopadhyay, T.Ideker, S.P.Goff, N.J.Krogan, A.D.Frankel, J.A.Young, and S.K.Chanda (2009).
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19194444 G.Cardone, J.G.Purdy, N.Cheng, R.C.Craven, and A.C.Steven (2009).
Visualization of a missing link in retrovirus capsid assembly.
  Nature, 457, 694-698.  
19914170 I.J.Byeon, X.Meng, J.Jung, G.Zhao, R.Yang, J.Ahn, J.Shi, J.Concel, C.Aiken, P.Zhang, and A.M.Gronenborn (2009).
Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function.
  Cell, 139, 780-790.
PDB code: 2kod
19825045 J.L.Neira (2009).
The capsid protein of human immunodeficiency virus: designing inhibitors of capsid assembly.
  FEBS J, 276, 6110-6117.  
19319933 J.Schlegel, G.S.Armstrong, J.S.Redzic, F.Zhang, and E.Z.Eisenmesser (2009).
Characterizing and controlling the inherent dynamics of cyclophilin-A.
  Protein Sci, 18, 811-824.  
19176623 M.Aoki, D.J.Venzon, Y.Koh, H.Aoki-Ogata, T.Miyakawa, K.Yoshimura, K.Maeda, and H.Mitsuya (2009).
Non-cleavage site gag mutations in amprenavir-resistant human immunodeficiency virus type 1 (HIV-1) predispose HIV-1 to rapid acquisition of amprenavir resistance but delay development of resistance to other protease inhibitors.
  J Virol, 83, 3059-3068.  
19455277 N.Sakamoto, and M.Watanabe (2009).
New therapeutic approaches to hepatitis C virus.
  J Gastroenterol, 44, 643-649.  
  19356241 S.Abdurahman, A.Végvári, M.Levi, S.Höglund, M.Högberg, W.Tong, I.Romero, J.Balzarini, and A.Vahlne (2009).
Isolation and characterization of a small antiretroviral molecule affecting HIV-1 capsid morphology.
  Retrovirology, 6, 34.  
  19254360 S.Matsuoka, E.Dam, D.Lecossier, F.Clavel, and A.J.Hance (2009).
Modulation of HIV-1 infectivity and cyclophilin A-dependence by Gag sequence and target cell type.
  Retrovirology, 6, 21.  
19116253 T.Miura, M.A.Brockman, A.Schneidewind, M.Lobritz, F.Pereyra, A.Rathod, B.L.Block, Z.L.Brumme, C.J.Brumme, B.Baker, A.C.Rothchild, B.Li, A.Trocha, E.Cutrell, N.Frahm, C.Brander, I.Toth, E.J.Arts, T.M.Allen, and B.D.Walker (2009).
HLA-B57/B*5801 human immunodeficiency virus type 1 elite controllers select for rare gag variants associated with reduced viral replication capacity and strong cytotoxic T-lymphotye recognition.
  J Virol, 83, 2743-2755.  
19262010 T.Nagao, K.Hatcho, N.Doi, S.Fujiwara, A.Adachi, and M.Nomaguchi (2009).
Amino acid alterations in Gag that confer the ability to grow in simian cells on HIV-1 are located at a narrow CA region.
  J Med Invest, 56, 21-25.  
19199580 X.Yu, Q.Wang, J.C.Yang, I.Buch, C.J.Tsai, B.Ma, S.Z.Cheng, R.Nussinov, and J.Zheng (2009).
Mutational analysis and allosteric effects in the HIV-1 capsid protein carboxyl-terminal dimerization domain.
  Biomacromolecules, 10, 390-399.  
19903261 Y.Kitagawa, M.Maeda-Sato, K.Tanaka, M.Tobiume, H.Sawa, H.Hasegawa, A.Kojima, W.W.Hall, T.Kurata, T.Sata, and H.Takahashi (2009).
Covalent bonded Gag multimers in human immunodeficiency virus type-1 particles.
  Microbiol Immunol, 53, 609-620.  
19656870 Y.Li, A.K.Kar, and J.Sodroski (2009).
Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A.
  J Virol, 83, 10951-10962.  
18385228 A.Schneidewind, M.A.Brockman, J.Sidney, Y.E.Wang, H.Chen, T.J.Suscovich, B.Li, R.I.Adam, R.L.Allgaier, B.R.Mothé, T.Kuntzen, C.Oniangue-Ndza, A.Trocha, X.G.Yu, C.Brander, A.Sette, B.D.Walker, and T.M.Allen (2008).
Structural and functional constraints limit options for cytotoxic T-lymphocyte escape in the immunodominant HLA-B27-restricted epitope in human immunodeficiency virus type 1 capsid.
  J Virol, 82, 5594-5605.  
18406133 B.K.Ganser-Pornillos, M.Yeager, and W.I.Sundquist (2008).
The structural biology of HIV assembly.
  Curr Opin Struct Biol, 18, 203-217.  
18287034 C.A.Virgen, Z.Kratovac, P.D.Bieniasz, and T.Hatziioannou (2008).
Independent genesis of chimeric TRIM5-cyclophilin proteins in two primate species.
  Proc Natl Acad Sci U S A, 105, 3563-3568.  
18799573 C.R.Langelier, V.Sandrin, D.M.Eckert, D.E.Christensen, V.Chandrasekaran, S.L.Alam, C.Aiken, J.C.Olsen, A.K.Kar, J.G.Sodroski, and W.I.Sundquist (2008).
Biochemical characterization of a recombinant TRIM5alpha protein that restricts human immunodeficiency virus type 1 replication.
  J Virol, 82, 11682-11694.  
18385230 F.Yang, J.M.Robotham, H.B.Nelson, A.Irsigler, R.Kenworthy, and H.Tang (2008).
Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro.
  J Virol, 82, 5269-5278.  
18057233 H.O.Peters, M.G.Mendoza, R.E.Capina, M.Luo, X.Mao, M.Gubbins, N.J.Nagelkerke, I.Macarthur, B.B.Sheardown, J.Kimani, C.Wachihi, S.Thavaneswaran, and F.A.Plummer (2008).
An integrative bioinformatic approach for studying escape mutations in human immunodeficiency virus type 1 gag in the Pumwani Sex Worker Cohort.
  J Virol, 82, 1980-1992.  
18577167 H.Takeuchi, and T.Matano (2008).
Host factors involved in resistance to retroviral infection.
  Microbiol Immunol, 52, 318-325.  
18443296 J.A.Readinger, G.M.Schiralli, J.K.Jiang, C.J.Thomas, A.August, A.J.Henderson, and P.L.Schwartzberg (2008).
Selective targeting of ITK blocks multiple steps of HIV replication.
  Proc Natl Acad Sci U S A, 105, 6684-6689.  
18489586 L.A.Alcaraz, M.Del Alamo, M.G.Mateu, and J.L.Neira (2008).
Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein.
  FEBS J, 275, 3299-3311.  
  18613956 L.Carthagena, M.C.Parise, M.Ringeard, M.K.Chelbi-Alix, U.Hazan, and S.Nisole (2008).
Implication of TRIM alpha and TRIMCyp in interferon-induced anti-retroviral restriction activities.
  Retrovirology, 5, 59.  
19092998 M.A.Rits, K.A.van Dort, and N.A.Kootstra (2008).
Polymorphisms in the regulatory region of the Cyclophilin A gene influence the susceptibility for HIV-1 infection.
  PLoS ONE, 3, e3975.  
18191978 M.Qi, and C.Aiken (2008).
Nef enhances HIV-1 infectivity via association with the virus assembly complex.
  Virology, 373, 287-297.  
18829762 M.Qi, R.Yang, and C.Aiken (2008).
Cyclophilin A-dependent restriction of human immunodeficiency virus type 1 capsid mutants for infection of nondividing cells.
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18275818 N.London, and O.Schueler-Furman (2008).
Funnel hunting in a rough terrain: learning and discriminating native energy funnels.
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18433823 P.M.Lokhandwala, T.L.Nguyen, J.B.Bowzard, and R.C.Craven (2008).
Cooperative role of the MHR and the CA dimerization helix in the maturation of the functional retrovirus capsid.
  Virology, 376, 191-198.  
18212100 R.G.Ptak, P.A.Gallay, D.Jochmans, A.P.Halestrap, U.T.Ruegg, L.A.Pallansch, M.D.Bobardt, Béthune, J.Neyts, E.De Clercq, J.M.Dumont, P.Scalfaro, K.Besseghir, R.M.Wenger, and B.Rosenwirth (2008).
Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin binding agent.
  Antimicrob Agents Chemother, 52, 1302-1317.  
  18605989 S.Brun, M.Solignat, B.Gay, E.Bernard, L.Chaloin, D.Fenard, C.Devaux, N.Chazal, and L.Briant (2008).
VSV-G pseudotyping rescues HIV-1 CA mutations that impair core assembly or stability.
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18382677 S.K.Kyere, P.R.Joseph, and M.F.Summers (2008).
The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
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18305041 S.Kawada, T.Goto, H.Haraguchi, A.Ono, and Y.Morikawa (2008).
Dominant negative inhibition of human immunodeficiency virus particle production by the nonmyristoylated form of gag.
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18678385 T.Y.Lin, and M.Emerman (2008).
Determinants of cyclophilin A-dependent TRIM5 alpha restriction against HIV-1.
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18385235 Y.Zhou, L.Rong, J.Lu, Q.Pan, and C.Liang (2008).
Insulin-like growth factor II mRNA binding protein 1 associates with Gag protein of human immunodeficiency virus type 1, and its overexpression affects virus assembly.
  J Virol, 82, 5683-5692.  
17804494 A.Schneidewind, M.A.Brockman, R.Yang, R.I.Adam, B.Li, S.Le Gall, C.R.Rinaldo, S.L.Craggs, R.L.Allgaier, K.A.Power, T.Kuntzen, C.S.Tung, M.X.LaBute, S.M.Mueller, T.Harrer, A.J.McMichael, P.J.Goulder, C.Aiken, C.Brander, A.D.Kelleher, and T.M.Allen (2007).
Escape from the dominant HLA-B27-restricted cytotoxic T-lymphocyte response in Gag is associated with a dramatic reduction in human immunodeficiency virus type 1 replication.
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17923088 B.K.Ganser-Pornillos, A.Cheng, and M.Yeager (2007).
Structure of full-length HIV-1 CA: a model for the mature capsid lattice.
  Cell, 131, 70-79.
PDB code: 3dik
18172386 C.H.Liao, Y.Q.Kuang, H.L.Liu, Y.T.Zheng, and B.Su (2007).
A novel fusion gene, TRIM5-Cyclophilin A in the pig-tailed macaque determines its susceptibility to HIV-1 infection.
  AIDS, 21, S19-S26.  
17715216 C.Song, and C.Aiken (2007).
Analysis of human cell heterokaryons demonstrates that target cell restriction of cyclosporine-resistant human immunodeficiency virus type 1 mutants is genetically dominant.
  J Virol, 81, 11946-11956.  
  17963512 D.M.Lang (2007).
Imperfect DNA mirror repeats in the gag gene of HIV-1 (HXB2) identify key functional domains and coincide with protein structural elements in each of the mature proteins.
  Virol J, 4, 113.  
17265140 E.Burkala, and M.Poss (2007).
Evolution of feline immunodeficiency virus Gag proteins.
  Virus Genes, 35, 251-264.  
17920096 F.Diaz-Griffero, A.Kar, M.Lee, M.Stremlau, E.Poeschla, and J.Sodroski (2007).
Comparative requirements for the restriction of retrovirus infection by TRIM5alpha and TRIMCyp.
  Virology, 369, 400-410.  
17574642 H.Javanbakht, F.Diaz-Griffero, W.Yuan, D.F.Yeung, X.Li, B.Song, and J.Sodroski (2007).
The ability of multimerized cyclophilin A to restrict retrovirus infection.
  Virology, 367, 19-29.  
16956947 J.Luban (2007).
Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type 1 infection.
  J Virol, 81, 1054-1061.  
17526561 L.A.Alcaraz, M.del Alamo, F.N.Barrera, M.G.Mateu, and J.L.Neira (2007).
Flexibility in HIV-1 assembly subunits: solution structure of the monomeric C-terminal domain of the capsid protein.
  Biophys J, 93, 1264-1276.
PDB code: 2jo0
17442718 L.S.Larsen, M.Zhang, N.Beliakova-Bethell, V.Bilanchone, A.Lamsa, K.Nagashima, R.Najdi, K.Kosaka, V.Kovacevic, J.Cheng, P.Baldi, G.W.Hatfield, and S.Sandmeyer (2007).
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PDB codes: 1em9 1eoq
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PDB codes: 1e6j 1e6o
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FKBP12 physically and functionally interacts with aspartokinase in Saccharomyces cerevisiae.
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PDB codes: 1awq 1awr 1aws 1awt 1awu 1awv
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Cryo-electron microscopy structure of yeast Ty retrotransposon virus-like particles.
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Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein.
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PDB codes: 1a8o 1am3 1aum
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