PDBsum entry 1ahd

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protein dna_rna links
DNA binding protein/DNA PDB id
Protein chain
68 a.a. *
* Residue conservation analysis
PDB id:
Name: DNA binding protein/DNA
Title: Determination of the nmr solution structure of an antennapedia homeodomain-DNA complex
Structure: DNA (5'- d( Gp Ap Ap Ap Gp Cp Cp Ap Tp Tp Ap Gp Ap G)-3'). Chain: a. Engineered: yes. DNA (5'- d( Cp Tp Cp Tp Ap Ap Tp Gp Gp Cp Tp Tp Tp C)-3'). Chain: b. Engineered: yes. Antennapedia protein mutant.
Source: Synthetic: yes. Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Organ: fruit. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 16 models
Authors: M.Billeter,Y.Q.Qian,G.Otting,M.Muller,W.J.Gehring,K.Wuthrich
Key ref: M.Billeter et al. (1993). Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex. J Mol Biol, 234, 1084-1093. PubMed id: 7903398
02-Apr-93     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P02833  (ANTP_DROME) -  Homeotic protein antennapedia
378 a.a.
68 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     regulation of transcription, DNA-dependent   1 term 
  Biochemical function     transcription regulatory region sequence-specific DNA binding     4 terms  


J Mol Biol 234:1084-1093 (1993)
PubMed id: 7903398  
Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex.
M.Billeter, Y.Q.Qian, G.Otting, M.Müller, W.Gehring, K.Wüthrich.
The nuclear magnetic resonance (NMR) solution structure of a complex formed by the mutant Antennapedia homeodomain with Cys39 replaced by Ser, Antp(C39S), and a 14 base-pair DNA duplex containing the BS2 operator sequence was determined using uniform 13C and 15N-labeling of the protein. Two-dimensional nuclear Overhauser enhancement spectroscopy ([1H,1H]NOESY) with 15N(omega 2)-half-filter and 13C(omega 1, omega 2)-double-half-filter, and three-dimensional heteronuclear-correlated [1H,1H]NOESY yielded a total of 855 intramolecular NOE upper distance constraints in the homeodomain, 151 upper distance constraints within the DNA duplex, and 39 intermolecular protein-DNA upper distance constraints. These data were used as the input for the structure calculation with simulated annealing followed by molecular dynamics in a water bath and energy refinement. A group of 16 conformers was thus generated which represent the solution structure of the Antp(C39S) homeodomain-DNA complex. The new structure determination confirms the salient features reported previously from a preliminary investigation of the same complex, in particular the location of the recognition helix in the major groove with the turn of the helix-turn-helix motif outside the contact area with the DNA, and the N-terminal arm of the homeodomain contacting the minor groove of the DNA. In addition, distinct amino acid side-chain-DNA contacts could be identified, and evidence was found that the invariant residue Asn51 (and possibly also Gln50) is in a slow dynamic equilibrium between two or several different DNA contact sites. The molecular dynamics calculations in a water bath yielded structures with hydration water molecules in the protein-DNA interface, which coincides with direct NMR observations of hydration waters. In the Appendix the experimental data obtained with the Antp(C39S) homeodomain-DNA complex and the techniques used for the structure calculation are evaluated using a simulated input data set derived from the X-ray crystal structure of a DNA complex with a homologous homeodomain. This study indicates that a nearly complete set of NOE upper distance constraints for the Antp(C39S) homeodomain and the protein-DNA interface was presently obtained. It further shows that the structure calculation used here yields a precise reproduction of the crystal structure from the simulated input data, and also results in hydration of the protein-DNA interface in the recalculated complex.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21071403 P.L.Privalov, A.I.Dragan, and C.Crane-Robinson (2011).
Interpreting protein/DNA interactions: distinguishing specific from non-specific and electrostatic from non-electrostatic components.
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21078959 D.Vuzman, and Y.Levy (2010).
DNA search efficiency is modulated by charge composition and distribution in the intrinsically disordered tail.
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20389279 K.Miyazono, Y.Zhi, Y.Takamura, K.Nagata, K.Saigo, T.Kojima, and M.Tanokura (2010).
Cooperative DNA-binding and sequence-recognition mechanism of aristaless and clawless.
  EMBO J, 29, 1613-1623.
PDB codes: 3a01 3a02 3a03 3lnq
20334529 R.Rohs, X.Jin, S.M.West, R.Joshi, B.Honig, and R.S.Mann (2010).
Origins of specificity in protein-DNA recognition.
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19666017 J.Clements, K.Hens, S.Merugu, B.Dichtl, Couet, and P.Callaerts (2009).
Mutational analysis of the eyeless gene and phenotypic rescue reveal that an intact Eyeless protein is necessary for normal eye and brain development in Drosophila.
  Dev Biol, 334, 503-512.  
19293143 L.Sivanantharajah, and A.Percival-Smith (2009).
Analysis of the Sequence and Phenotype of Drosophila Sex combs reduced Alleles Reveals Potential Functions of Conserved Protein Motifs of the Sex combs reduced Protein.
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18816799 T.A.Ramelot, S.Raman, A.P.Kuzin, R.Xiao, L.C.Ma, T.B.Acton, J.F.Hunt, G.T.Montelione, D.Baker, and M.A.Kennedy (2009).
Improving NMR protein structure quality by Rosetta refinement: a molecular replacement study.
  Proteins, 75, 147-167.
PDB codes: 1tvg 1xpw
18931781 G.M.Clore (2008).
Visualizing lowly-populated regions of the free energy landscape of macromolecular complexes by paramagnetic relaxation enhancement.
  Mol Biosyst, 4, 1058-1069.  
17496025 D.Shental-Bechor, T.Haliloglu, and N.Ben-Tal (2007).
Interactions of cationic-hydrophobic peptides with lipid bilayers: a Monte Carlo simulation method.
  Biophys J, 93, 1858-1871.  
17981120 R.Joshi, J.M.Passner, R.Rohs, R.Jain, A.Sosinsky, M.A.Crickmore, V.Jacob, A.K.Aggarwal, B.Honig, and R.S.Mann (2007).
Functional specificity of a Hox protein mediated by the recognition of minor groove structure.
  Cell, 131, 530-543.
PDB codes: 2r5y 2r5z
16839862 F.Liu, F.A.Ismat, and V.V.Patel (2006).
Role of homeodomain-only protein in the cardiac conduction system.
  Trends Cardiovasc Med, 16, 193-198.  
16642002 J.Iwahara, and G.M.Clore (2006).
Detecting transient intermediates in macromolecular binding by paramagnetic NMR.
  Nature, 440, 1227-1230.  
15931687 K.U.Schneider, A.Marchini, N.Sabherwal, R.Röth, B.Niesler, T.Marttila, R.J.Blaschke, M.Lawson, M.Dumic, and G.Rappold (2005).
Alteration of DNA binding, dimerization, and nuclear translocation of SHOX homeodomain mutations identified in idiopathic short stature and Leri-Weill dyschondrosteosis.
  Hum Mutat, 26, 44-52.  
15542560 M.F.Lensink, B.Christiaens, J.Vandekerckhove, A.Prochiantz, and M.Rosseneu (2005).
Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase.
  Biophys J, 88, 939-952.  
16075387 Z.N.Akin, and A.J.Nazarali (2005).
Hox genes and their candidate downstream targets in the developing central nervous system.
  Cell Mol Neurobiol, 25, 697-741.  
15468320 A.Gutmanas, and M.Billeter (2004).
Specific DNA recognition by the Antp homeodomain: MD simulations of specific and nonspecific complexes.
  Proteins, 57, 772-782.  
15103611 S.B.Nabuurs, A.J.Nederveen, W.Vranken, J.F.Doreleijers, A.M.Bonvin, G.W.Vuister, G.Vriend, and C.A.Spronk (2004).
DRESS: a database of REfined solution NMR structures.
  Proteins, 55, 483-486.  
12538894 A.Ke, and C.Wolberger (2003).
Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera.
  Protein Sci, 12, 306-312.
PDB codes: 1mh3 1mh4
12595558 A.Nijnik, R.Mott, D.P.Kwiatkowski, and I.A.Udalova (2003).
Comparing the fine specificity of DNA binding by NF-kappaB p50 and p52 using principal coordinates analysis.
  Nucleic Acids Res, 31, 1497-1501.  
12493834 M.Zeeb, and J.Balbach (2003).
Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization.
  Protein Sci, 12, 112-123.  
12923056 N.A.LaRonde-LeBlanc, and C.Wolberger (2003).
Structure of HoxA9 and Pbx1 bound to DNA: Hox hexapeptide and DNA recognition anterior to posterior.
  Genes Dev, 17, 2060-2072.
PDB code: 1puf
12297045 F.Chen, H.Kook, R.Milewski, A.D.Gitler, M.M.Lu, J.Li, R.Nazarian, R.Schnepp, K.Jen, C.Biben, G.Runke, J.P.Mackay, J.Novotny, R.J.Schwartz, R.P.Harvey, M.C.Mullins, and J.A.Epstein (2002).
Hop is an unusual homeobox gene that modulates cardiac development.
  Cell, 110, 713-723.  
11867548 J.Iwahara, M.Iwahara, G.W.Daughdrill, J.Ford, and R.T.Clubb (2002).
The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA.
  EMBO J, 21, 1197-1209.
PDB code: 1kqq
11668629 A.V.D'Elia, G.Tell, I.Paron, L.Pellizzari, R.Lonigro, and G.Damante (2001).
Missense mutations of human homeoboxes: A review.
  Hum Mutat, 18, 361-374.  
11391564 G.Iurcu-Mustata, D.Van Belle, R.Wintjens, M.Prévost, and M.Rooman (2001).
Role of salt bridges in homeodomains investigated by structural analyses and molecular dynamics simulations.
  Biopolymers, 59, 145-159.  
11738049 T.Nishikawa, H.Okamura, A.Nagadoi, P.König, D.Rhodes, and Y.Nishimura (2001).
Solution structure of a telomeric DNA complex of human TRF1.
  Structure, 9, 1237-1251.
PDB codes: 1ity 1iv6
10882080 D.Niessing, W.Driever, F.Sprenger, H.Taubert, H.Jäckle, and R.Rivera-Pomar (2000).
Homeodomain position 54 specifies transcriptional versus translational control by Bicoid.
  Mol Cell, 5, 395-401.  
  11058088 J.T.Bryan, and M.I.Morasso (2000).
The Dlx3 protein harbors basic residues required for nuclear localization, transcriptional activity and binding to Msx1.
  J Cell Sci, 113, 4013-4023.  
10889025 R.A.Grant, M.A.Rould, J.D.Klemm, and C.O.Pabo (2000).
Exploring the role of glutamine 50 in the homeodomain-DNA interface: crystal structure of engrailed (Gln50 --> ala) complex at 2.0 A.
  Biochemistry, 39, 8187-8192.
PDB code: 1du0
10799563 R.G.Mirmira, H.Watada, and M.S.German (2000).
Beta-cell differentiation factor Nkx6.1 contains distinct DNA binding interference and transcriptional repression domains.
  J Biol Chem, 275, 14743-14751.  
11003663 V.Dave, C.Zhao, F.Yang, C.S.Tung, and J.Ma (2000).
Reprogrammable recognition codes in bicoid homeodomain-DNA interaction.
  Mol Cell Biol, 20, 7673-7684.  
10410794 C.Wolberger (1999).
Multiprotein-DNA complexes in transcriptional regulation.
  Annu Rev Biophys Biomol Struct, 28, 29-56.  
10543441 D.Mennerich, S.Hoffmann, T.Hadrys, H.H.Arnold, and E.Bober (1999).
Two highly related homeodomain proteins, Nkx5-1 and Nkx5-2, display different DNA binding specificities.
  Biol Chem, 380, 1041-1048.  
9876118 F.Fogolari, P.Zuccato, G.Esposito, and P.Viglino (1999).
Biomolecular electrostatics with the linearized Poisson-Boltzmann equation.
  Biophys J, 76, 1.  
10605826 G.Tell, R.Acquaviva, S.Formisano, F.Fogolari, C.Pucillo, and G.Damante (1999).
Comparative stability analysis of the thyroid transcription factor 1 and Antennapedia homeodomains: evidence for residue 54 in controlling the structural stability of the recognition helix.
  Int J Biochem Cell Biol, 31, 1339-1353.  
  10523646 K.Shanmugam, N.C.Green, I.Rambaldi, H.U.Saragovi, and M.S.Featherstone (1999).
PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX proteins.
  Mol Cell Biol, 19, 7577-7588.  
10336376 R.Schleif (1999).
Arm-domain interactions in proteins: a review.
  Proteins, 34, 1-3.  
10512803 S.Sen, and L.Nilsson (1999).
Structure, interaction, dynamics and solvent effects on the DNA-EcoRI complex in aqueous solution from molecular dynamics simulation.
  Biophys J, 77, 1782-1800.  
  10082571 T.Kophengnavong, A.S.Carroll, and T.K.Blackwell (1999).
The SKN-1 amino-terminal arm is a DNA specificity segment.
  Mol Cell Biol, 19, 3039-3050.  
10465734 W.S.Tzou, and M.J.Hwang (1999).
Modeling helix-turn-helix protein-induced DNA bending with knowledge-based distance restraints.
  Biophys J, 77, 1191-1205.  
  9858582 Y.Jin, H.Zhong, and A.K.Vershon (1999).
The yeast a1 and alpha2 homeodomain proteins do not contribute equally to heterodimeric DNA binding.
  Mol Cell Biol, 19, 585-593.  
9521728 A.Hall, I.Ekiel, R.W.Mason, F.Kasprzykowski, A.Grubb, and M.Abrahamson (1998).
Structural basis for different inhibitory specificities of human cystatins C and D.
  Biochemistry, 37, 4071-4079.  
9451007 J.Iwahara, T.Kigawa, K.Kitagawa, H.Masumoto, T.Okazaki, and S.Yokoyama (1998).
A helix-turn-helix structure unit in human centromere protein B (CENP-B).
  EMBO J, 17, 827-837.
PDB code: 1bw6
9565750 J.P.Schneider, A.Lombardi, and W.F.DeGrado (1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
  Fold Des, 3, R29-R40.  
9736626 M.D.Allen, K.Yamasaki, M.Ohme-Takagi, M.Tateno, and M.Suzuki (1998).
A novel mode of DNA recognition by a beta-sheet revealed by the solution structure of the GCC-box binding domain in complex with DNA.
  EMBO J, 17, 5484-5496.
PDB codes: 1gcc 2gcc 3gcc
9699631 S.A.Dames, R.A.Kammerer, R.Wiltscheck, J.Engel, and A.T.Alexandrescu (1998).
NMR structure of a parallel homotrimeric coiled coil.
  Nat Struct Biol, 5, 687-691.
PDB code: 1aq5
9556579 S.Weiler, J.M.Gruschus, D.H.Tsao, L.Yu, L.H.Wang, M.Nirenberg, and J.A.Ferretti (1998).
Site-directed mutations in the vnd/NK-2 homeodomain. Basis of variations in structure and sequence-specific DNA binding.
  J Biol Chem, 273, 10994-11000.  
9204277 D.E.Wemmer, and P.B.Dervan (1997).
Targeting the minor groove of DNA.
  Curr Opin Struct Biol, 7, 355-361.  
9241421 G.Patikoglou, and S.K.Burley (1997).
Eukaryotic transcription factor-DNA complexes.
  Annu Rev Biophys Biomol Struct, 26, 289-325.  
  9144767 H.Li, R.Tejero, D.Monleon, D.Bassolino-Klimas, C.Abate-Shen, R.E.Bruccoleri, and G.T.Montelione (1997).
Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: application in predicting the three-dimensional structure of murine homeodomain Msx-1.
  Protein Sci, 6, 956-970.  
9154919 J.M.Gruschus, D.H.Tsao, L.H.Wang, M.Nirenberg, and J.A.Ferretti (1997).
Interactions of the vnd/NK-2 homeodomain with DNA by nuclear magnetic resonance spectroscopy: basis of binding specificity.
  Biochemistry, 36, 5372-5380.
PDB codes: 1nk2 1nk3
9032063 J.W.Schwabe (1997).
The role of water in protein-DNA interactions.
  Curr Opin Struct Biol, 7, 126-134.  
9188697 L.Li, and K.S.Matthews (1997).
Differences in water release with DNA binding by ultrabithorax and deformed homeodomains.
  Biochemistry, 36, 7003-7011.  
9309220 L.Tucker-Kellogg, M.A.Rould, K.A.Chambers, S.E.Ades, R.T.Sauer, and C.O.Pabo (1997).
Engrailed (Gln50-->Lys) homeodomain-DNA complex at 1.9 A resolution: structural basis for enhanced affinity and altered specificity.
  Structure, 5, 1047-1054.
PDB code: 2hdd
9365251 M.C.Justice, B.P.Hogan, and A.K.Vershon (1997).
Homeodomain-DNA interactions of the Pho2 protein are promoter-dependent.
  Nucleic Acids Res, 25, 4730-4739.  
9253405 M.P.Foster, D.S.Wuttke, I.Radhakrishnan, D.A.Case, J.M.Gottesfeld, and P.E.Wright (1997).
Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.
  Nat Struct Biol, 4, 605-608.
PDB code: 1tf3
9056723 P.Callaerts, G.Halder, and W.J.Gehring (1997).
PAX-6 in development and evolution.
  Annu Rev Neurosci, 20, 483-532.  
9053397 W.D.Kohn, C.T.Mant, and R.S.Hodges (1997).
Alpha-helical protein assembly motifs.
  J Biol Chem, 272, 2583-2586.  
8768898 A.J.Wand, and S.W.Englander (1996).
Protein complexes studied by NMR spectroscopy.
  Curr Opin Biotechnol, 7, 403-408.  
8768896 A.K.Vershon (1996).
Protein interactions of homeodomain proteins.
  Curr Opin Biotechnol, 7, 392-396.  
8702862 A.Zhu, and M.A.Kuziora (1996).
Homeodomain interaction with the beta subunit of the general transcription factor TFIIE.
  J Biol Chem, 271, 20993-20996.  
  8657149 C.P.Chang, L.Brocchieri, W.F.Shen, C.Largman, and M.L.Cleary (1996).
Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus.
  Mol Cell Biol, 16, 1734-1745.  
8696974 C.Wolberger (1996).
Homeodomain interactions.
  Curr Opin Struct Biol, 6, 62-68.  
8811078 D.Fabbro, G.Tell, A.Leonardi, L.Pellizzari, C.Pucillo, R.Lonigro, S.Formisano, and G.Damante (1996).
In the TTF-1 homeodomain the contribution of several amino acids to DNA recognition depends on the bound sequence.
  Nucleic Acids Res, 24, 3283-3288.  
8692913 D.S.Wilson, G.Sheng, S.Jun, and C.Desplan (1996).
Conservation and diversification in homeodomain-DNA interactions: a comparative genetic analysis.
  Proc Natl Acad Sci U S A, 93, 6886-6891.  
  8890172 G.Damante, L.Pellizzari, G.Esposito, F.Fogolari, P.Viglino, D.Fabbro, G.Tell, S.Formisano, and R.Di Lauro (1996).
A molecular code dictates sequence-specific DNA recognition by homeodomains.
  EMBO J, 15, 4992-5000.  
8898894 G.Esposito, F.Fogolari, G.Damante, S.Formisano, G.Tell, A.Leonardi, R.Di Lauro, and P.Viglino (1996).
Analysis of the solution structure of the homeodomain of rat thyroid transcription factor 1 by 1H-NMR spectroscopy and restrained molecular mechanics.
  Eur J Biochem, 241, 101-113.
PDB code: 1ftt
8679635 H.Thorogood, T.R.Waters, A.W.Parker, C.W.Wharton, and B.A.Connolly (1996).
Resonance Raman spectroscopy of 4-thiothymidine and oligodeoxynucleotides containing this base both free in solution and bound to the restriction endonuclease EcoRV.
  Biochemistry, 35, 8723-8733.  
8703957 L.Li, D.von Kessler, P.A.Beachy, and K.S.Matthews (1996).
pH-dependent enhancement of DNA binding by the ultrabithorax homeodomain.
  Biochemistry, 35, 9832-9839.  
  8698039 L.T.Peltenburg, and C.Murre (1996).
Engrailed and Hox homeodomain proteins contain a related Pbx interaction motif that recognizes a common structure present in Pbx.
  EMBO J, 15, 3385-3393.  
8620531 P.Konig, R.Giraldo, L.Chapman, and D.Rhodes (1996).
The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA.
  Cell, 85, 125-136.
PDB code: 1ign
  8665855 S.K.Chan, H.Pöpperl, R.Krumlauf, and R.S.Mann (1996).
An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif.
  EMBO J, 15, 2476-2487.  
8643557 S.K.Chan, and R.S.Mann (1996).
A structural model for a homeotic protein-extradenticle-DNA complex accounts for the choice of HOX protein in the heterodimer.
  Proc Natl Acad Sci U S A, 93, 5223-5228.  
8943030 T.E.Haerry, and W.J.Gehring (1996).
Intron of the mouse Hoxa-7 gene contains conserved homeodomain binding sites that can function as an enhancer element in Drosophila.
  Proc Natl Acad Sci U S A, 93, 13884-13889.  
  8575189 A.M.Gronenborn, and G.M.Clore (1995).
Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy.
  Crit Rev Biochem Mol Biol, 30, 351-385.  
7671301 D.S.Wilson, B.Guenther, C.Desplan, and J.Kuriyan (1995).
High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA.
  Cell, 82, 709-719.
PDB code: 1fjl
  7613470 E.H.Morita, M.Shirakawa, F.Hayashi, M.Imagawa, and Y.Kyogoku (1995).
Structure of the Oct-3 POU-homeodomain in solution, as determined by triple resonance heteronuclear multidimensional NMR spectroscopy.
  Protein Sci, 4, 729-739.
PDB code: 1ocp
  8557047 J.A.Hirsch, and A.K.Aggarwal (1995).
Structure of the even-skipped homeodomain complexed to AT-rich DNA: new perspectives on homeodomain specificity.
  EMBO J, 14, 6280-6291.
PDB code: 1jgg
7568211 J.L.Pomerantz, C.O.Pabo, and P.A.Sharp (1995).
Analysis of homeodomain function by structure-based design of a transcription factor.
  Proc Natl Acad Sci U S A, 92, 9752-9756.  
  8563623 N.D.Clarke (1995).
Covariation of residues in the homeodomain sequence family.
  Protein Sci, 4, 2269-2278.  
7487967 R.S.Mann (1995).
The specificity of homeotic gene function.
  Bioessays, 17, 855-863.  
8591025 T.Tullius (1995).
Homeodomains: together again for the first time.
  Structure, 3, 1143-1145.  
7915030 G.Damante, D.Fabbro, L.Pellizzari, D.Civitareale, S.Guazzi, M.Polycarpou-Schwartz, S.Cauci, F.Quadrifoglio, S.Formisano, and R.Di Lauro (1994).
Sequence-specific DNA recognition by the thyroid transcription factor-1 homeodomain.
  Nucleic Acids Res, 22, 3075-3083.  
  7849596 N.D.Clarke, C.R.Kissinger, J.Desjarlais, G.L.Gilliland, and C.O.Pabo (1994).
Structural studies of the engrailed homeodomain.
  Protein Sci, 3, 1779-1787.
PDB code: 1enh
7765166 S.Campbell-Burk, and S.Zhong (1994).
Biomolecular applications of heteronuclear multidimensional NMR.
  Curr Opin Biotechnol, 5, 346-354.  
8044836 W.J.Gehring, Y.Q.Qian, M.Billeter, K.Furukubo-Tokunaga, A.F.Schier, D.Resendez-Perez, M.Affolter, G.Otting, and K.Wüthrich (1994).
Homeodomain-DNA recognition.
  Cell, 78, 211-223.  
7909611 Y.Q.Qian, D.Resendez-Perez, W.J.Gehring, and K.Wüthrich (1994).
The des(1-6)antennapedia homeodomain: comparison of the NMR solution structure and the DNA-binding affinity with the intact Antennapedia homeodomain.
  Proc Natl Acad Sci U S A, 91, 4091-4095.
PDB code: 1san
7915838 Z.Shang, V.E.Isaac, H.Li, L.Patel, K.M.Catron, T.Curran, G.T.Montelione, and C.Abate (1994).
Design of a "minimAl" homeodomain: the N-terminal arm modulates DNA binding affinity and stabilizes homeodomain structure.
  Proc Natl Acad Sci U S A, 91, 8373-8377.  
16100952 A.Fede, M.Billeter, W.Leupin, and K.Wüthrich (1993).
Determination of the NMR solution structure of the Hoechst 33258-d(GTGGAATTCCAC)2 complex and comparison with the X-ray crystal structure.
  Structure, 1, 177-186.  
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 codes are shown on the right.