Crystallization, sequence, and preliminary crystallographic data for an antipeptide Fab 50.1 and peptide complexes with the principal neutralizing determinant of HIV-1 gpl20

X‐ray quality crystals of an Fab fragment from an antipeptide monoclonal antibody (R/V3‐50.1) that recognizes the principal neutralizing determinant (PND) of the gpl20 glycoprotein of human immunodeficiency virus type 1 (HIV‐1) (MN isolate) were grown as uncomplexed and peptide complexed forms. Crys...

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Veröffentlicht in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1992-12, Vol.14 (4), p.499-508
Hauptverfasser: Sturam, Enrico A., Stanfield, Robyn L., Fieser, Gail G., Silver, Sandra, Roguska, Michael, Hincapie, L. Marina, Simmerman, Heather K. B., Profy, Albert T., Wilson, Ian A.
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container_end_page 508
container_issue 4
container_start_page 499
container_title Proteins, structure, function, and bioinformatics
container_volume 14
creator Sturam, Enrico A.
Stanfield, Robyn L.
Fieser, Gail G.
Silver, Sandra
Roguska, Michael
Hincapie, L. Marina
Simmerman, Heather K. B.
Profy, Albert T.
Wilson, Ian A.
description X‐ray quality crystals of an Fab fragment from an antipeptide monoclonal antibody (R/V3‐50.1) that recognizes the principal neutralizing determinant (PND) of the gpl20 glycoprotein of human immunodeficiency virus type 1 (HIV‐1) (MN isolate) were grown as uncomplexed and peptide complexed forms. Crystals of the free Fab grew from high salt in orthorhombic space groups P212121 and I222 and from polyethylene glycol in space groups P1 and P21. Seeds from either the P1 and P21 native (uncomplexed) Fab crystals induced nucleation of crystals of the Fab complexed to a 16‐residue synthetic peptide corresponding to the PND when streak seeded into preequilibrated solutions of this complex. Data were collected from these complex crystals and from each of the four native Fab forms to at least 2.8Å resolution. The genes for the variable domain of the Fab were cloned and sequenced and the primary amino acid sequence was deduced from this information. Knowledge of the three‐dimensional structure of this Fab–pep‐tide complex will be important in the understanding of the PND of HIV‐1 and its recognition by neutralizing monoclonal antibodies. © 1992 Wiley‐Liss, Inc.
doi_str_mv 10.1002/prot.340140410
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subjects antipeptide antibody
Fab sequence
HIV-1
PEG crystallization
principal neutralizing determinant
protein crystallization
X-ray crystallography
title Crystallization, sequence, and preliminary crystallographic data for an antipeptide Fab 50.1 and peptide complexes with the principal neutralizing determinant of HIV-1 gpl20
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