Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
about
Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites3D domain swapping: a mechanism for oligomer assemblyRefined structure of dimeric diphtheria toxin at 2.0 A resolutionA comprehensive analysis of 40 blind protein structure predictions.Protein design: toward functional metalloenzymesThe structural basis of repertoire shift in an immune response to phosphocholineProline in α-helical kink is required for folding kinetics but not for kinked structure, function, or stability of heat shock transcription factorThe crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP coreAn ancestral nuclear protein assembly: Crystal structure of theMethanopyrus kandlerihistoneX-Ray Crystal Structures of Human Immunodeficiency Virus Type 1 Protease Mutants Complexed with AtazanavirCrystal structure of interleukin 8: symbiosis of NMR and crystallographyThe structure of human tau-tubulin kinase 1 both in the apo form and in complex with an inhibitorStructure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complexStructure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding proteinCrystal structure of an idiotype-anti-idiotype Fab complexCrystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen ELocation of a potential transport binding site in a sigma class glutathione transferase by x-ray crystallographyThe three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain.Crystal structure of fibrinogen-Aalpha peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolutionProtective natural autoantibodies to apoptotic cells: evidence of convergent selection of recurrent innate-like clonesA unified statistical framework for sequence comparison and structure comparisonEvidence for ligand-induced conformational changes in proteins from phosphorescence spectroscopy.The double edged sword of the immune response: mutational analysis of a murine anti-pneumococcal, anti-DNA antibodyCrystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNAA missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 A resolutionModeling the antigen combining site of an anti-dinitrophenyl antibody, ANO2.Comprehensive evaluation of protein structure alignment methods: scoring by geometric measures.BAYESIAN PROTEIN STRUCTURE ALIGNMENTGlutamate provides a key structural contact between reticulon-4 (Nogo-66) and phosphocholineImmunoglobulin VH clan and family identity predicts variable domain structure and may influence antigen binding.Generation and analysis of random point mutations in an antibody CDR2 sequence: many mutated antibodies lose their ability to bind antigenSynthetic antibody libraries focused towards peptide ligands.Variable region framework differences result in decreased or increased affinity of variant anti-digoxin antibodies.Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coliModel-building study of the combining sites of two antibodies to alpha (1----6)dextran.Three-dimensional structure of Fab R19.9, a monoclonal murine antibody specific for the p-azobenzenearsonate groupA single amino acid substitution in the variable region of the light chain specifically blocks immunoglobulin secretionThe nature of cation-pi binding: interactions between tetramethylammonium ion and benzene in aqueous solutionSymmetry of Fv architecture is conducive to grafting a second antibody binding site in the Fv region.
P2860
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P2860
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
description
1986 nî lūn-bûn
@nan
1986 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
name
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@ast
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@en
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@nl
type
label
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@ast
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@en
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@nl
prefLabel
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@ast
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@en
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@nl
P2093
P1476
Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A
@en
P2093
P304
P356
10.1016/0022-2836(86)90245-7
P407
P577
1986-08-01T00:00:00Z