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PDBsum entry 1xtc

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protein Protein-protein interface(s) links
Toxin PDB id
1xtc
Jmol
Contents
Protein chains
192 a.a. *
45 a.a. *
103 a.a. *
Waters ×138
* Residue conservation analysis
PDB id:
1xtc
Name: Toxin
Title: Cholera toxin
Structure: Cholera toxin. Chain: a. Synonym: ctx, choleragen. Cholera toxin. Chain: c. Synonym: ctx, choleragen. Cholera toxin. Chain: d, e, f, g, h. Synonym: ctx, choleragen
Source: Vibrio cholerae. Organism_taxid: 44104. Strain: 569b. Other_details: commercially obtained from list biological laboratory, campber ca95008. Laboratory, campber ca95008
Biol. unit: Heptamer (from PQS)
Resolution:
2.40Å     R-factor:   0.185    
Authors: R.-G.Zhang,E.Westbrook
Key ref:
R.G.Zhang et al. (1995). The three-dimensional crystal structure of cholera toxin. J Mol Biol, 251, 563-573. PubMed id: 7658473 DOI: 10.1006/jmbi.1995.0456
Date:
10-Jan-96     Release date:   01-Aug-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01555  (CHTA_VIBCH) -  Cholera enterotoxin subunit A
Seq:
Struc:
258 a.a.
192 a.a.*
Protein chain
Pfam   ArchSchema ?
P01555  (CHTA_VIBCH) -  Cholera enterotoxin subunit A
Seq:
Struc:
258 a.a.
45 a.a.
Protein chains
Pfam   ArchSchema ?
P01556  (CHTB_VIBCH) -  Cholera enterotoxin subunit B
Seq:
Struc:
124 a.a.
103 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   4 terms 
  Biological process     killing of cells of other organism   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
DOI no: 10.1006/jmbi.1995.0456 J Mol Biol 251:563-573 (1995)
PubMed id: 7658473  
 
 
The three-dimensional crystal structure of cholera toxin.
R.G.Zhang, D.L.Scott, M.L.Westbrook, S.Nance, B.D.Spangler, G.G.Shipley, E.M.Westbrook.
 
  ABSTRACT  
 
The clinical manifestations of cholera are largely attributable to the actions of a secreted hexameric AB5 enterotoxin (choleragen). We have independently solved and refined the three-dimensional structure of choleragen at 2.5 A resolution. The structure of the crystalline toxin closely resembles that described for the heat-labile enterotoxin from Escherichia coli (LT) with which it shares 80% sequence homology. In both cases, the wedge-shaped A subunit is loosely held high above the plane of the pentameric B subunits by the tethering A2 chain. The most striking difference between the two toxins occurs at the carboxyl terminus of the A2 chain. Whereas the last 14 residues of the A2 chain of LT threading through the central pore of the B5 assembly form an extended chain with a terminal loop, the A2 chain of choleragen remains a nearly continuous alpha-helix throughout its length. The four carboxyl-terminal residues of the A2 chain (KDEL sequence), disordered in the crystal structure of LT, are clearly visible in choleragen's electron-density map. In the accompanying article we describe the three-dimensional structure of the isolated B pentamer of cholera toxin (choleragenoid). Comparison of the crystalline coordinates of choleragen, choleragenoid, and LT provides a solid three-dimensional foundation for further experimental investigation. These structures, along with those of related toxins from Shigella dysenteria and Bordetella pertussis, offer a first step towards the rational design of new vaccines and anti-microbial agents.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Representative electron-density for cholera toxin. Stereo view of the 2Fo--Fc electron-density map at the junction between the A subunit and the B pentamer. The long A2 a-helix (orange) can be seen as it begins its descent into the central pore. Residues belonging to the A1 chain or to the B pentamer are indicated (Pro120 and Ala(4)75, respectively).
Figure 9.
Figure 9. Cross-section through the central ``channel'' of choleragen. The A1 chain, A2 chain, and the B subunits are colored cyan, gold, and lavender, respectively. Side-chains contributing to the A2/B interface are shaded according to charge potential: green, non-polar; red, negatively charged; blue, positively charged. The Trp88 of opposed B subunits are shown to assist with orientation. Yellow spheres represent well-resolved water molecules. TheA2/B interface is initially quite non-polar but becomes quite polar deeper in the channel. The carboxyl terminus of the A2 chain presumably interacts with the surface of the membrane during GM1 binding. The sequence of the terminal four residues (KDEL) is identical to that shown to act as endoplasmic retention signal (Lewis & Pelham, 1990; Joseph et al., 1978, 1979).
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1995, 251, 563-573) copyright 1995.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21474780 E.B.Watkins, C.E.Miller, J.Majewski, and T.L.Kuhl (2011).
Membrane texture induced by specific protein binding and receptor clustering: active roles for lipids in cellular function.
  Proc Natl Acad Sci U S A, 108, 6975-6980.  
21041954 D.E.Saslowsky, J.A.Cho, H.Chinnapen, R.H.Massol, D.J.Chinnapen, J.S.Wagner, H.E.De Luca, W.Kam, B.H.Paw, and W.I.Lencer (2010).
Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2.
  J Clin Invest, 120, 4399-4409.  
21203571 J.Zrimi, A.Ng Ling, E.Giri-Rachman Arifin, G.Feverati, and C.Lesieur (2010).
Cholera toxin B subunits assemble into pentamers--proposition of a fly-casting mechanism.
  PLoS One, 5, e15347.  
20860656 S.Ramasamy, C.Q.Liu, H.Tran, A.Gubala, P.Gauci, J.McAllister, and T.Vo (2010).
Principles of antidote pharmacology: an update on prophylaxis, post-exposure treatment recommendations and research initiatives for biological agents.
  Br J Pharmacol, 161, 721-748.  
19289469 M.L.Forster, J.J.Mahn, and B.Tsai (2009).
Generating an Unfoldase from Thioredoxin-like Domains.
  J Biol Chem, 284, 13045-13056.  
18359802 C.E.Miller, J.Majewski, E.B.Watkins, and T.L.Kuhl (2008).
Part I: an x-ray scattering study of cholera toxin penetration and induced phase transformations in lipid membranes.
  Biophys J, 95, 629-640.  
18515100 G.Zhang (2008).
Design, synthesis, and evaluation of bisubstrate analog inhibitors of cholera toxin.
  Bioorg Med Chem Lett, 18, 3724-3727.  
18349144 J.Baysarowich, K.Koteva, D.W.Hughes, L.Ejim, E.Griffiths, K.Zhang, M.Junop, and G.D.Wright (2008).
Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr.
  Proc Natl Acad Sci U S A, 105, 4886-4891.
PDB code: 2hw2
17962948 M.K.Sharma, N.K.Singh, D.Jani, R.Sisodia, M.Thungapathra, J.K.Gautam, L.S.Meena, Y.Singh, A.Ghosh, A.K.Tyagi, and A.K.Sharma (2008).
Expression of toxin co-regulated pilus subunit A (TCPA) of Vibrio cholerae and its immunogenic epitopes fused to cholera toxin B subunit in transgenic tomato (Solanum lycopersicum).
  Plant Cell Rep, 27, 307-318.  
18618297 M.Oszvald, T.J.Kang, S.Tomoskozi, B.Jenes, T.G.Kim, Y.S.Cha, L.Tamas, and M.S.Yang (2008).
Expression of cholera toxin B subunit in transgenic rice endosperm.
  Mol Biotechnol, 40, 261-268.  
18272180 R.S.Ampapathi, A.L.Creath, D.I.Lou, J.W.Craft, S.R.Blanke, and G.B.Legge (2008).
Order-disorder-order transitions mediate the activation of cholera toxin.
  J Mol Biol, 377, 748-760.  
17976649 A.H.Pande, P.Scaglione, M.Taylor, K.N.Nemec, S.Tuthill, D.Moe, R.K.Holmes, S.A.Tatulian, and K.Teter (2007).
Conformational instability of the cholera toxin A1 polypeptide.
  J Mol Biol, 374, 1114-1128.  
17728161 D.M.Owen, M.A.Neil, P.M.French, and A.I.Magee (2007).
Optical techniques for imaging membrane lipid microdomains in living cells.
  Semin Cell Dev Biol, 18, 591-598.  
17526733 J.Kato, J.Zhu, C.Liu, and J.Moss (2007).
Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice.
  Mol Cell Biol, 27, 5534-5543.  
17712773 P.Scheerer, A.Kramer, L.Otte, M.Seifert, H.Wessner, C.Scholz, N.Krauss, J.Schneider-Mergener, and W.Höhne (2007).
Structure of an anti-cholera toxin antibody Fab in complex with an epitope-derived D-peptide: a case of polyspecific recognition.
  J Mol Recognit, 20, 263-274.
PDB code: 1zea
17280480 S.Sakaguchi, and T.Arakawa (2007).
Recent developments in mucosal vaccines against prion diseases.
  Expert Rev Vaccines, 6, 75-85.  
17931161 T.D.Connell (2007).
Cholera toxin, LT-I, LT-IIa and LT-IIb: the critical role of ganglioside binding in immunomodulation by type I and type II heat-labile enterotoxins.
  Expert Rev Vaccines, 6, 821-834.  
17325057 T.Shimizu, S.Kawakami, T.Sato, T.Sasaki, M.Higashide, T.Hamabata, T.Ohta, and M.Noda (2007).
The serine 31 residue of the B subunit of Shiga toxin 2 is essential for secretion in enterohemorrhagic Escherichia coli.
  Infect Immun, 75, 2189-2200.  
16931513 A.R.Morrison, J.Moss, L.A.Stevens, J.E.Evans, C.Farrell, E.Merithew, D.G.Lambright, D.L.Greiner, J.P.Mordes, A.A.Rossini, and R.Bortell (2006).
ART2, a T cell surface mono-ADP-ribosyltransferase, generates extracellular poly(ADP-ribose).
  J Biol Chem, 281, 33363-33372.  
16728322 D.R.Hill, L.Ford, and D.G.Lalloo (2006).
Oral cholera vaccines: use in clinical practice.
  Lancet Infect Dis, 6, 361-373.  
16461395 J.P.Williams, D.C.Smith, B.N.Green, B.D.Marsden, K.R.Jennings, L.M.Roberts, and J.H.Scrivens (2006).
Gas phase characterization of the noncovalent quaternary structure of cholera toxin and the cholera toxin B subunit pentamer.
  Biophys J, 90, 3246-3254.  
16956368 K.P.Holbourn, C.C.Shone, and K.R.Acharya (2006).
A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins.
  FEBS J, 273, 4579-4593.  
16552056 K.Teter, M.G.Jobling, D.Sentz, and R.K.Holmes (2006).
The cholera toxin A1(3) subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol.
  Infect Immun, 74, 2259-2267.  
  16511307 S.Kernstock, F.Koch-Nolte, J.Mueller-Dieckmann, M.S.Weiss, and C.Mueller-Dieckmann (2006).
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 224-227.  
16099990 C.J.O'Neal, M.G.Jobling, R.K.Holmes, and W.G.Hol (2005).
Structural basis for the activation of cholera toxin by human ARF6-GTP.
  Science, 309, 1093-1096.
PDB codes: 2a5d 2a5f 2a5g
15812247 R.S.Blumberg, R.S.Pitman, C.T.Taylor, and S.P.Colgan (2005).
Cholera toxin potentiates influences of IFN-gamma through activation of NF-kappaB and release of tumor necrosis factor-alpha.
  J Interferon Cytokine Res, 25, 209-219.  
16113283 T.Harakuni, H.Sugawa, A.Komesu, M.Tadano, and T.Arakawa (2005).
Heteropentameric cholera toxin B subunit chimeric molecules genetically fused to a vaccine antigen induce systemic and mucosal immune responses: a potential new strategy to target recombinant vaccine antigens to mucosal immune systems.
  Infect Immun, 73, 5654-5665.  
15189866 C.E.Miller, J.Majewski, R.Faller, S.Satija, and T.L.Kuhl (2004).
Cholera toxin assault on lipid monolayers containing ganglioside GM1.
  Biophys J, 86, 3700-3708.  
15458407 L.H.Coye, and C.M.Collins (2004).
Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes.
  Mol Microbiol, 54, 89-98.  
12721285 C.Bourgeois, I.Okazaki, E.Cavanaugh, M.Nightingale, and J.Moss (2003).
Identification of regulatory domains in ADP-ribosyltransferase-1 that determine transferase and NAD glycohydrolase activities.
  J Biol Chem, 278, 26351-26355.  
12704173 F.Biet, L.Kremer, I.Wolowczuk, M.Delacre, and C.Locht (2003).
Immune response induced by recombinant Mycobacterium bovis BCG producing the cholera toxin B subunit.
  Infect Immun, 71, 2933-2937.  
12819100 J.K.Tinker, J.L.Erbe, W.G.Hol, and R.K.Holmes (2003).
Cholera holotoxin assembly requires a hydrophobic domain at the A-B5 interface: mutational analysis and development of an in vitro assembly system.
  Infect Immun, 71, 4093-4101.  
13679513 Y.Fujinaga, A.A.Wolf, C.Rodighiero, H.Wheeler, B.Tsai, L.Allen, M.G.Jobling, T.Rapoport, R.K.Holmes, and W.I.Lencer (2003).
Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm.
  Mol Biol Cell, 14, 4783-4793.  
11877421 C.Lesieur, M.J.Cliff, R.Carter, R.F.James, A.R.Clarke, and T.R.Hirst (2002).
A kinetic model of intermediate formation during assembly of cholera toxin B-subunit pentamers.
  J Biol Chem, 277, 16697-16704.  
12089141 J.Sánchez, G.Wallerström, M.Fredriksson, J.Angström, and J.Holmgren (2002).
Detoxification of cholera toxin without removal of its immunoadjuvanticity by the addition of (STa-related) peptides to the catalytic subunit. A potential new strategy to generate immunostimulants for vaccination.
  J Biol Chem, 277, 33369-33377.  
11854209 M.G.Jobling, and R.K.Holmes (2002).
Mutational analysis of ganglioside GM(1)-binding ability, pentamer formation, and epitopes of cholera toxin B (CTB) subunits and CTB/heat-labile enterotoxin B subunit chimeras.
  Infect Immun, 70, 1260-1271.  
11290330 B.Tsai, C.Rodighiero, W.I.Lencer, and T.A.Rapoport (2001).
Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin.
  Cell, 104, 937-948.  
11251877 C.P.Simmons, M.Ghaem-Magami, L.Petrovska, L.Lopes, B.M.Chain, N.A.Williams, and G.Dougan (2001).
Immunomodulation using bacterial enterotoxins.
  Scand J Immunol, 53, 218-226.  
11551401 L.C.Norkin (2001).
Caveolae in the uptake and targeting of infectious agents and secreted toxins.
  Adv Drug Deliv Rev, 49, 301-315.  
11698663 M.E.Scott, Z.Y.Dossani, and M.Sandkvist (2001).
Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway.
  Proc Natl Acad Sci U S A, 98, 13978-13983.  
11395467 M.G.Jobling, and R.K.Holmes (2001).
Biological and biochemical characterization of variant A subunits of cholera toxin constructed by site-directed mutagenesis.
  J Bacteriol, 183, 4024-4032.  
11349009 M.Sandkvist (2001).
Type II secretion and pathogenesis.
  Infect Immun, 69, 3523-3535.  
11705889 S.Wimer-Mackin, R.K.Holmes, A.A.Wolf, W.I.Lencer, and M.G.Jobling (2001).
Characterization of receptor-mediated signal transduction by Escherichia coli type IIa heat-labile enterotoxin in the polarized human intestinal cell line T84.
  Infect Immun, 69, 7205-7212.  
10940245 D.S.Goodsell, and A.J.Olson (2000).
Structural symmetry and protein function.
  Annu Rev Biophys Biomol Struct, 29, 105-153.  
10972829 H.Otto, D.Tezcan-Merdol, R.Girisch, F.Haag, M.Rhen, and F.Koch-Nolte (2000).
The spvB gene-product of the Salmonella enterica virulence plasmid is a mono(ADP-ribosyl)transferase.
  Mol Microbiol, 37, 1106-1115.  
11095841 J.Yu, and W.H.Langridge (2000).
Novel Approaches to Oral Vaccines: Delivery of Antigens by Edible Plants.
  Curr Infect Dis Rep, 2, 73-77.  
10620294 K.Saxena, P.Zimmermann, R.R.Schmidt, and G.G.Shipley (2000).
Bilayer properties of totally synthetic C16:0-lactosyl-ceramide.
  Biophys J, 78, 306-312.  
11106366 M.G.Jobling, and R.K.Holmes (2000).
Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system.
  Proc Natl Acad Sci U S A, 97, 14662-14667.  
9933586 C.Rodighiero, A.T.Aman, M.J.Kenny, J.Moss, W.I.Lencer, and T.R.Hirst (1999).
Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity.
  J Biol Chem, 274, 3962-3969.  
  10085117 D.Matković-Calogović, A.Loregian, M.R.D'Acunto, R.Battistutta, A.Tossi, G.Palù, and G.Zanotti (1999).
Crystal structure of the B subunit of Escherichia coli heat-labile enterotoxin carrying peptides with anti-herpes simplex virus type 1 activity.
  J Biol Chem, 274, 8764-8769.
PDB codes: 1b44 1ltr
  11138935 S.M.Kavic, E.J.Frehm, and A.S.Segal (1999).
Case studies in cholera: lessons in medical history and science.
  Yale J Biol Med, 72, 393-408.  
10398406 S.V.Evans, and C.Roger MacKenzie (1999).
Characterization of protein-glycolipid recognition at the membrane bilayer.
  J Mol Recognit, 12, 155-168.  
10231518 W.E.Minke, C.Roach, W.G.Hol, and C.L.Verlinde (1999).
Structure-based exploration of the ganglioside GM1 binding sites of Escherichia coli heat-labile enterotoxin and cholera toxin for the discovery of receptor antagonists.
  Biochemistry, 38, 5684-5692.  
10395933 W.I.Lencer, T.R.Hirst, and R.K.Holmes (1999).
Membrane traffic and the cellular uptake of cholera toxin.
  Biochim Biophys Acta, 1450, 177-190.  
9585411 A.A.Wolf, M.G.Jobling, S.Wimer-Mackin, M.Ferguson-Maltzman, J.L.Madara, R.K.Holmes, and W.I.Lencer (1998).
Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia.
  J Cell Biol, 141, 917-927.  
9521710 A.Ruf, G.de Murcia, and G.E.Schulz (1998).
Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling.
  Biochemistry, 37, 3893-3900.
PDB codes: 2paw 2pax 3pax 4pax
9914258 D.B.Lacy, and R.C.Stevens (1998).
Unraveling the structures and modes of action of bacterial toxins.
  Curr Opin Struct Biol, 8, 778-784.  
9789264 G.Del Giudice, M.Pizza, and R.Rappuoli (1998).
Molecular basis of vaccination.
  Mol Aspects Med, 19, 1.  
  9753491 J.L.Turvill, F.H.Mourad, and M.J.Farthing (1998).
Crucial role for 5-HT in cholera toxin but not Escherichia coli heat-labile enterotoxin-intestinal secretion in rats.
  Gastroenterology, 115, 883-890.  
9576414 J.P.Raufman (1998).
Cholera.
  Am J Med, 104, 386-394.  
9682972 L.Agren, B.Löwenadler, and N.Lycke (1998).
A novel concept in mucosal adjuvanticity: the CTA1-DD adjuvant is a B cell-targeted fusion protein that incorporates the enzymatically active cholera toxin A1 subunit.
  Immunol Cell Biol, 76, 280-287.  
9682971 L.de Haan, W.Verweij, E.Agsteribbe, and J.Wilschut (1998).
The role of ADP-ribosylation and G(M1)-binding activity in the mucosal immunogenicity and adjuvanticity of the Escherichia coli heat-labile enterotoxin and Vibrio cholerae cholera toxin.
  Immunol Cell Biol, 76, 270-279.  
9572842 M.Degano, S.C.Almo, J.C.Sacchettini, and V.L.Schramm (1998).
Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor.
  Biochemistry, 37, 6277-6285.
PDB code: 2mas
  9786724 O.Lundgren (1998).
5-Hydroxytryptamine, enterotoxins, and intestinal fluid secretion.
  Gastroenterology, 115, 1009-1012.  
9333321 B.Hazes, and R.J.Read (1997).
Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells.
  Biochemistry, 36, 11051-11054.  
9012663 C.E.Bell, and D.Eisenberg (1997).
Crystal structure of nucleotide-free diphtheria toxin.
  Biochemistry, 36, 481-488.
PDB code: 1sgk
9384564 E.A.Merritt, S.Sarfaty, I.K.Feil, and W.G.Hol (1997).
Structural foundation for the design of receptor antagonists targeting Escherichia coli heat-labile enterotoxin.
  Structure, 5, 1485-1499.
PDB codes: 1lt5 1lt6
  9416616 F.van den Akker, I.K.Feil, C.Roach, A.A.Platas, E.A.Merritt, and W.G.Hol (1997).
Crystal structure of heat-labile enterotoxin from Escherichia coli with increased thermostability introduced by an engineered disulfide bond in the A subunit.
  Protein Sci, 6, 2644-2649.
PDB code: 1lt3
  9416617 F.van den Akker, M.Pizza, R.Rappuoli, and W.G.Hol (1997).
Crystal structure of a non-toxic mutant of heat-labile enterotoxin, which is a potent mucosal adjuvant.
  Protein Sci, 6, 2650-2654.
PDB code: 1lt4
9230049 J.A.McCann, J.A.Mertz, J.Czworkowski, and W.D.Picking (1997).
Conformational changes in cholera toxin B subunit-ganglioside GM1 complexes are elicited by environmental pH and evoke changes in membrane structure.
  Biochemistry, 36, 9169-9178.  
9218785 J.Rossjohn, J.T.Buckley, B.Hazes, A.G.Murzin, R.J.Read, and M.W.Parker (1997).
Aerolysin and pertussis toxin share a common receptor-binding domain.
  EMBO J, 16, 3426-3434.  
9138559 O.S.Smart, J.Breed, G.R.Smith, and M.S.Sansom (1997).
A novel method for structure-based prediction of ion channel conductance properties.
  Biophys J, 72, 1109-1126.  
9315851 V.Rolli, M.O'Farrell, J.Ménissier-de Murcia, and G.de Murcia (1997).
Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching.
  Biochemistry, 36, 12147-12154.  
8755499 A.Ruf, J.Mennissier de Murcia, G.de Murcia, and G.E.Schulz (1996).
Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
  Proc Natl Acad Sci U S A, 93, 7481-7485.
PDB codes: 1paw 1pax
8805549 F.van den Akker, S.Sarfaty, E.M.Twiddy, T.D.Connell, R.K.Holmes, and W.G.Hol (1996).
Crystal structure of a new heat-labile enterotoxin, LT-IIb.
  Structure, 4, 665-678.
PDB code: 1tii
8901582 K.Sandvig, O.Garred, and B.van Deurs (1996).
Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum.
  Proc Natl Acad Sci U S A, 93, 12339-12343.  
8973177 L.W.Ruddock, H.M.Webb, S.P.Ruston, C.Cheesman, R.B.Freedman, and T.R.Hirst (1996).
A pH-dependent conformational change in the B-subunit pentamer of Escherichia coli heat-labile enterotoxin: structural basis and possible functional role for a conserved feature of the AB5 toxin family.
  Biochemistry, 35, 16069-16076.  
8702586 L.W.Ruddock, J.J.Coen, C.Cheesman, R.B.Freedman, and T.R.Hirst (1996).
Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Kinetics and molecular basis of rate-limiting steps in vitro.
  J Biol Chem, 271, 19118-19123.  
8785291 R.A.Reed, and G.G.Shipley (1996).
Properties of ganglioside GM1 in phosphatidylcholine bilayer membranes.
  Biophys J, 70, 1363-1372.  
8921943 Y.Cong, H.R.Bowdon, and C.O.Elson (1996).
Identification of an immunodominant T cell epitope on cholera toxin.
  Eur J Immunol, 26, 2587-2594.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.