BIOMAT Database Logo BIOMAT Database Logo

Structure of an anti-HIV monoclonal Fab antibody fragment specific to a gp120 C-4 region peptide. 2001

M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
Department of Biochemistry and Cell Biology, Rice University, Houston, Texas, USA.

UI MeSH Term Description Entries
D007140 Immunoglobulin Fab Fragments Univalent antigen-binding fragments composed of one entire IMMUNOGLOBULIN LIGHT CHAIN and the amino terminal end of one of the IMMUNOGLOBULIN HEAVY CHAINS from the hinge region, linked to each other by disulfide bonds. Fab contains the IMMUNOGLOBULIN VARIABLE REGIONS, which are part of the antigen-binding site, and the first IMMUNOGLOBULIN CONSTANT REGIONS. This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN. Fab Fragment,Fab Fragments,Ig Fab Fragments,Immunoglobulins, Fab Fragment,Fab Immunoglobulin Fragments,Immunoglobulin Fab Fragment,Immunoglobulins, Fab,Fab Fragment Immunoglobulins,Fab Fragment, Immunoglobulin,Fab Fragments, Immunoglobulin,Fragment Immunoglobulins, Fab,Fragment, Fab,Immunoglobulin Fragments, Fab
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal
D000918 Antibody Specificity The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site. Antibody Specificities,Specificities, Antibody,Specificity, Antibody
D000939 Epitopes Sites on an antigen that interact with specific antibodies. Antigenic Determinant,Antigenic Determinants,Antigenic Specificity,Epitope,Determinant, Antigenic,Determinants, Antigenic,Specificity, Antigenic
D015483 HIV Antibodies Antibodies reactive with HIV ANTIGENS. AIDS Antibodies,HIV-Associated Antibodies,HTLV-III Antibodies,HTLV-III-LAV Antibodies,LAV Antibodies,Lymphadenopathy-Associated Antibodies,T-Lymphotropic Virus Type III Antibodies, Human,HIV Associated Antibodies,HTLV III Antibodies,HTLV III LAV Antibodies,Lymphadenopathy Associated Antibodies,T Lymphotropic Virus Type III Antibodies, Human,Antibodies, AIDS,Antibodies, HIV,Antibodies, HIV Associated,Antibodies, HIV-Associated,Antibodies, HTLV III,Antibodies, HTLV-III,Antibodies, HTLV-III-LAV,Antibodies, LAV,Antibodies, Lymphadenopathy Associated,Antibodies, Lymphadenopathy-Associated
D015699 HIV Envelope Protein gp120 External envelope protein of the human immunodeficiency virus which is encoded by the HIV env gene. It has a molecular weight of 120 kDa and contains numerous glycosylation sites. Gp120 binds to cells expressing CD4 cell-surface antigens, most notably T4-lymphocytes and monocytes/macrophages. Gp120 has been shown to interfere with the normal function of CD4 and is at least partly responsible for the cytopathic effect of HIV. Envelope Glycoprotein gp120, HIV,HTLV-III gp120,env Protein gp120, HIV,gp120(HIV),HIV Envelope Glycoprotein gp120,gp120 Envelope Glycoprotein, HIV,HTLV III gp120,gp120, HTLV-III

Related Publications

M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
Preliminary crystallographic analysis of the Fab fragment of an antibody against HIV gp120.
July 1990, Journal of molecular biology,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
Structure of the Fab fragment of a monoclonal antibody specific for carcinoembryonic antigen.
November 1996, Acta crystallographica. Section D, Biological crystallography,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
A monoclonal antibody Fab fragment crystallized with and without a peptide epitope from HIV.
August 1993, Proteins,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
[Cloning of human monoclonal Fab fragments against HIV-1 gp120 peptide binding chemokine receptor from phage Fab antibody library].
December 2002, Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
2.9 A resolution structure of an anti-dinitrophenyl-spin-label monoclonal antibody Fab fragment with bound hapten.
September 1991, Journal of molecular biology,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
Structure of a monoclonal anti-ICAM-1 antibody R6.5 Fab fragment at 2.8 A resolution.
May 1995, Acta crystallographica. Section D, Biological crystallography,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
Crystal structure of the liganded anti-gibberellin A(4) antibody 4-B8(8)/E9 Fab fragment.
April 2002, Biochemical and biophysical research communications,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
X-ray crystal structure of an anti-Buckminsterfullerene antibody fab fragment: biomolecular recognition of C(60).
October 2000, Proceedings of the National Academy of Sciences of the United States of America,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
Crystal structure and computational modeling of the fab fragment from a protective anti-ricin monoclonal antibody.
January 2012, PloS one,
M B Berry, and K A Johnson, and W Radding, and M Fung, and R Liou, and G N Phillips
Structure of the Fab fragment from a neutralizing monoclonal antibody directed against an epitope of gp41 from HIV-1.
March 1997, Acta crystallographica. Section D, Biological crystallography,
Copied contents to your clipboard!