(Q27622174)

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The crystal structure of the Fab fragment of a rat monoclonal antibody against the main immunogenic region of the human muscle acetylcholine receptor

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The crystal structure of the Fab fragment of a rat monoclonal antibody against the main immunogenic region of the human muscle acetylcholine receptor (English)

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crystal structure

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based on heuristic

inferred from title

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based on heuristic

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author name string

M Kontou

1

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D D Leonidas

2

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E H Vatzaki

3

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P Tsantili

4

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A Mamalaki

5

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N G Oikonomakos

6

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K R Acharya

7

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S J Tzartos

8

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language of work or name

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publication date

April 2000

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267

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8

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2389-97

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Monoclonal antibodies used to probe acetylcholine receptor structure: localization of the main immunogenic region and detection of similarities between subunits

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Anatomy of the antigenic structure of a large membrane autoantigen, the muscle-type nicotinic acetylcholine receptor

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Localization of the main immunogenic region of human muscle acetylcholine receptor to residues 67-76 of the alpha subunit

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Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data

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Fab fragments of monoclonal antibodies protect the human acetylcholine receptor against antigenic modulation caused by myasthenic sera

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Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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Local and transmitted conformational changes on complexation of an anti-sweetener Fab

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[32] Patterson correlation searches and refinement.

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Improved methods for building protein models in electron density maps and the location of errors in these models

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High affinity single-chain Fv antibody fragments protecting the human nicotinic acetylcholine receptor

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Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures.

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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PROCHECK: a program to check the stereochemical quality of protein structures

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Bound water molecules and conformational stabilization help mediate an antigen-antibody association

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Checking your imagination: applications of the free R value

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Conformation of Polypeptides and Proteins

1 reference

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Standard conformations for the canonical structures of immunoglobulins

1 reference

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Structure of an Fab fragment against a C-terminal peptide of hCG at 2.0 A resolution

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Genetically engineered immunoglobulins reveal structural features controlling segmental flexibility

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Conformations of immunoglobulin hypervariable regions

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Conformations of the third hypervariable region in the VH domain of immunoglobulins

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Conformation of the hypervariable region L3 without the key proline residue.

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Antibody-antigen interactions: contact analysis and binding site topography.

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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An extensively modified version of MolScript that includes greatly enhanced coloring capabilities

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Improved Fourier coefficients for maps using phases from partial structures with errors

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Myasthenia gravis

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Three-dimensional location of the main immunogenic region of the acetylcholine receptor

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High-resolution epitope mapping and fine antigenic characterization of the main immunogenic region of the acetylcholine receptor. Improving the binding activity of synthetic analogues of the region

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Conformational requirements for molecular recognition of acetylcholine receptor main immunogenic region (MIR) analogues by monoclonal anti-MIR antibody: a two-dimensional nuclear magnetic resonance and molecular dynamics approach

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Passive transfer of experimental myasthenia gravis via antigenic modulation of acetylcholine receptor

1 reference

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Characterisation, crystallisation and preliminary X-ray diffraction analysis of a Fab fragment of a rat monoclonal antibody with very high affinity for the human muscle acetylcholine receptor

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Canonical structures for the hypervariable regions of immunoglobulins

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Structural classification of CDR-H3 in antibodies

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On the nature of antibody combining sites: Unusual structural features that may confer on these sites an enhanced capacity for binding ligands

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Canonical structure repertoire of the antigen-binding site of immunoglobulins suggests strong geometrical restrictions associated to the mechanism of immune recognition

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10.1046/J.1432-1327.2000.01252.X

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