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1
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0026030568
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Chemistry and biology of the immunophilins and their immunosuppressive ligands
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(1991)
Science
, vol.251
, pp. 283-287
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Schreiber1
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2
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0000548829
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Three-dimensional structure of peptide-protein complexes: implications for recognition
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(1992)
Curr Opin Struct Biol
, vol.2
, pp. 904-919
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Marshall1
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3
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0000289157
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X-ray crystallographic studies of antibody-peptide complexes
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A thorough and detailed analysis of antibody-peptide interactions that highlights the different conformations of peptides bound to antibodies.
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(1993)
ImmunoMethods
, vol.3
, pp. 211-221
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Stanfield1
Wilson2
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4
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0028289241
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Anatomy of the antibody molecule
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An excellent and detailed review paper on antibodies that includes a comparison of antibody-peptide and protease-peptide interactions.
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(1994)
Mol Immunol
, vol.31
, pp. 169-217
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Padlan1
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10
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0027525106
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The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2
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A detailed comparison of how disparate peptide sequences can bind with high affinity to the same MHC class I molecule.
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(1993)
Cell
, vol.75
, pp. 693-708
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Madden1
Garboczi2
Wiley3
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11
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0028150789
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Three-dimensional structure of a peptide extending from one end of a class I MHC binding site
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Structural evidence for an alternative way that longer peptides can bind to MHC class I molecules by extending their C-terminal ends out of the binding groove rather than bulging out in the middle.
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(1994)
Nature
, vol.371
, pp. 626-629
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Collins1
Garboczi2
Wiley3
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12
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0028361575
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Five viral peptide-HLA-A2 co-crystals. Simultaneous space group determination and X-ray data collection
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(1994)
J Mol Biol
, vol.239
, pp. 581-587
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Garboczi1
Madden2
Wiley3
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13
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0027974989
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b at 2.4Åresolution: implications for antigen-determinant selection
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b different from other MHC class I molecules.
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(1994)
Cell
, vol.76
, pp. 39-50
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Young1
Zhang2
Sacchettini3
Nathenson4
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14
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0028348369
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Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
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The first single peptide complex of a class II molecule shows the peptide extending out of both ends of the binding groove. A different set of interactions between the MHC molecule and the peptide backbone (as compared to class I-peptide complexes) are used in order to keep the peptide in an extended conformation.
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(1994)
Nature
, vol.368
, pp. 215-221
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Stern1
Brown2
Jardetzky3
Gorga4
Urban5
Strominger6
Wiley7
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15
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0027745982
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Structural basis of pilus subunit recognition by the PapD chaperone
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This paper describes a novel use of two immunoglobulin-like domains in the periplasmic chaperone PapD to create a binding site for the recognition of the C-terminal sequences of pilus proteins.
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(1993)
Science
, vol.262
, pp. 1234-1241
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Kuehn1
Ogg2
Kihlberg3
Slonim4
Flemmer5
Bergfors6
Hultgren7
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16
-
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0028452862
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The structural basis of sequence-independent peptide binding by OppA protein
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A fascinating structure that takes 517 residues and a complex fold to produce an internal cavity that binds peptides of only two to five residues in a sequence-independent manner.
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(1994)
Science
, vol.264
, pp. 1578-1581
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Tame1
Murshudov2
Dodson3
Neil4
Dodson5
Higgins6
Wilkinson7
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18
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0027409064
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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms
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(1993)
Cell
, vol.72
, pp. 779-790
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Waksman1
Shoelson2
Pant3
Cowburn4
Kuriyan5
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20
-
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0028773467
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Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
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The binding of different peptides to the SH2 domain of a tyrosine phosphatase (Syp) is similar to that of the SH2 domains of tyrosine kinases Src and Lck, but with a more extensive interface.
-
(1994)
Structure
, vol.2
, pp. 423-438
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Lee1
Kominos2
Jacques3
Margolis4
Schlessinger5
Shoelson6
Kuriyan7
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21
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0028337397
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Structure of the regulatory domains of the Src-family tyrosine kinase Lck
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This structure of the SH2–SH3 regulatory domains shows how peptide interacts with both domains and suggests that dimerization at the SH2–SH3 interface may be involved in regulation of the Src family of kinases.
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(1994)
Nature
, vol.368
, pp. 764-769
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Eck1
Atwell2
Shoelson3
Harrison4
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22
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0013484134
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Structural basis for the binding of proline-rich peptides to SH3 domains
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An extensive study that highlights the solution structure for the P13K SH3 domain in a complex with a proline-rich peptide selected from a combinatorial peptide library. Also included are the results from the peptide library screening, and some mutational analysis of the SH3 domain, and mutational analysis of the peptide used in the structure to determine the relative importance of each residue for binding.
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(1994)
Cell
, vol.76
, pp. 933-945
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Yu1
Chen2
Feng3
Dalgarno4
Brauer5
Schreiber6
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23
-
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0028485085
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High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
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The X-ray crystal structures are reported here for two SH3 domains from the Abl and Fyn tyrosine kinases in complex with peptides. The peptides both adopt a left-handed polyproline type II helix conformation in the complexes.
-
(1994)
Nature Struct Biol
, vol.1
, pp. 546-551
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Musacchio1
Saraste2
Wilmanns3
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24
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0027962645
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Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions
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The NMR solution structures for two SH3 domains in complex with different (class I and class II) peptides. The different classes of peptides have arginine residues at opposite ends, resulting in the binding of the peptides to SH3 in opposite directions. The arginine residue in each peptide forms a salt bridge with a conserved aspartate residue in the SH3 domain. Each peptide maintains a left-handed polyproline type II helical conformation.
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(1994)
Science
, vol.266
, pp. 1241-1247
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Feng1
Chen2
Yu3
Simon4
Schreiber5
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28
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0026794065
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Target enzyme recognition by calmodulin: 2.4Åstructure of a calmodulin-peptide complex
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(1992)
Science
, vol.257
, pp. 1251-1255
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Meador1
Means2
Quiocho3
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29
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0027759276
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Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
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Comparison of different peptides bound to calmodulin shows how the central helix of calmodulin can unwind in order to adapt and expand to fit different sequences of helical peptides.
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(1993)
Science
, vol.262
, pp. 1718-1721
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Meador1
Means2
Quiocho3
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32
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0026532051
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A conformation of cyclosporin A in aqueous environment revealed by the X-ray structure of a cyclosporin-Fab complex
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(1992)
Science
, vol.256
, pp. 92-94
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Altschuh1
Vix2
Rees3
Thierry4
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33
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0027462844
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Crystallographic analysis of the interaction between Cyclosporin A and the Fab fragment of a monoclonal antibody
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(1993)
Proteins
, vol.15
, pp. 339-348
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Vix1
Rees2
Thierry3
Altschuh4
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34
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0027301875
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Crystal structure of an anticholera toxin peptide complex at 2.3Å
-
(1993)
J Mol Biol
, vol.232
, pp. 1169-1175
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Shoham1
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36
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0027133936
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Detailed analysis of the free and bound conformations of an antibody. X-ray structures of Fab 17/9 and three different Fab-peptide complexes
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Extensive analysis of the conformations of peptides of different lengths bound to an anti-peptide antibody. The peptide conformation has a strong resemblance to its counterpart in the intact influenza virus hemagglutinin.
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(1993)
J Mol Biol
, vol.234
, pp. 1098-1118
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Schulze-Gahmen1
Rini2
Wilson3
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37
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0028024259
-
Crystal structure of a peptide complex of anti-influenza peptide antibody Fab 26/9. Comparison of two different antibodies bound to the same peptide antigen
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The conformation of a peptide bound to two different but related anti-peptide Fabs is similar in the two structures, but there are slight rearrangements in the Fab 26/9 binding site that include a water molecule in the antibody-peptide interface.
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(1994)
J Mol Biol
, vol.241
, pp. 534-556
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Churchill1
Stura2
Pinilla3
Appel4
Houghten5
Kono6
Balderas7
Fieser8
Schulze-Gahmen9
Wilson10
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38
-
-
0028327101
-
Crystal structure of the principal neutralization site of HIV-1
-
Surprisingly, the V3 loop peptide from HIV-1 gp120 adopts a double turn at the crown of the loop when bound to Fab 59.1. A comparison with another V3 loop peptide bound to Fab 50.1 has enabled a more detailed structure for the V3 loop to be pieced together from the two Fab-peptide complexes.
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(1994)
Science
, vol.264
, pp. 82-85
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Ghiara1
Stura2
Stanfield3
Profy4
Wilson5
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39
-
-
0028304866
-
Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2
-
The structure of the bound peptide consists of an Asn-pseudoturn following a type I ß-turn. The authors discuss the resemblance of the peptide's conformation to that of the peptide at the equivalent position in the closely related HRV1A virus and go on to compare the structure to that of the unliganded Fab.
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(1994)
EMBO J
, vol.13
, pp. 2247-2256
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Tormo1
Blaas2
Parry3
Rowlands4
Stuart5
Fita6
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43
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0028470793
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Antigen-induced conformational changes in antibodies: a problem for structural prediction and design
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(1994)
Trends Biotechnol
, vol.12
, pp. 275-279
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Stanfield1
Wilson2
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46
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0026802451
-
Crystal structure of a streptococcal protein G domain bound to an Fab fragment
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(1992)
Nature
, vol.359
, pp. 752-754
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Derrick1
Wigley2
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47
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0028352702
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Calmodulin interacts with amphiphilic peptides composed of all d-amino acids
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Binding data for d-melittin and d-smooth muscle light-chain kinase peptides rather surprisingly show that they bind avidly to calmodulin and probably occupy the same binding site as l-peptides.
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(1994)
Nature
, vol.368
, pp. 651-653
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Fisher1
Prendergast2
Ehrhardt3
Urbauer4
Wand5
Sedarous6
McCormick7
Buckley8
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48
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0026794581
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The three-dimensional structure of HLA-B27 at 2.1Åresolution suggests a general mechanism for tight peptide binding MHC
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(1992)
Cell
, vol.70
, pp. 1035-1048
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Madden1
Gorga2
Strominger3
Wiley4
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50
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0028131363
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Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules
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Reconstitution experiments and thermal denaturation studies with non-amer peptides modified at their termini show that the charge interactions contribute more to the stabilization of the HLA-A2 complex than the anchor positions.
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(1994)
Science
, vol.265
, pp. 398-402
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Bouvier1
Wiley2
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52
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0028773294
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Antigenic peptide binding by class I and class II histocompatibility proteins
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Excellent minireview of the general similarities and differences of peptide binding to MHC class I and class II molecules.
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(1994)
Structure
, vol.2
, pp. 245-251
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Stern1
Wiley2
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53
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0026244229
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure
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(1991)
J Appl Crystallogr
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, pp. 946-950
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Kraulis1
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57
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0000541786
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Some methods for examining the interaction between two molecules
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(1993)
ImmunoMethods
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, pp. 191-196
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Sheriff1
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58
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0021755764
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Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect
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(1984)
J Mol Biol
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, pp. 63-89
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Richmond1
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59
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0015222647
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The interpretation of protein structures: estimation of static accessibility
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(1971)
J Mol Biol
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Lee1
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60
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0021107965
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Solvent-accessible surfaces of proteins and nucleic acids
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(1983)
Science
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, pp. 709-713
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Connolly1
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