Till sidans topp

Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12

Tipsa en vän
Utskriftsversion

Crystal structure of the … - Göteborgs universitet Till startsida
Webbkarta
Till innehåll Läs mer om hur kakor används på gu.se

Crystal structure of the HIV-2 neutralizing Fab fragment 7C8 with high specificity to the V3 region of gp125.

Artikel i vetenskaplig tidskrift
Författare Hannes Uchtenhagen
Rosmarie Friemann
Grzegorz Raszewski
Anna-Lena Spetz
Lennart Nilsson
Adnane Achour
Publicerad i PloS one
Volym 6
Nummer/häfte 4
Sidor e18767
ISSN 1932-6203
Publiceringsår 2011
Publicerad vid Institutionen för kemi
Sidor e18767
Språk en
Länkar dx.doi.org/10.1371/journal.pone.001...
Ämnesord Amino Acid Sequence, Animals, Antibodies, Monoclonal, chemistry, immunology, Antibodies, Neutralizing, chemistry, immunology, Antibody Specificity, immunology, Binding Sites, Complementarity Determining Regions, chemistry, immunology, Computer Simulation, Crystallography, X-Ray, Epitopes, chemistry, immunology, HIV-2, immunology, Humans, Hydrophobic and Hydrophilic Interactions, Immunoglobulin Fab Fragments, chemistry, immunology, Mice, Models, Molecular, Molecular Sequence Data, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, env Gene Products, Human Immunodeficiency Virus, chemistry, immunology
Ämneskategorier Strukturbiologi

Sammanfattning

7C8 is a mouse monoclonal antibody specific for the third hypervariable region (V3) of the human immunodeficiency virus type 2 (HIV-2)-associated protein gp125. The three-dimensional crystal structure of the Fab fragment of 7C8, determined to 2.7 Å resolution, reveals a deep and narrow antigen-binding cleft with architecture appropriate for an elongated epitope. The highly hydrophobic cleft is bordered on one side by the negatively charged second complementarity determining region (CDR2) and the unusually long positively charged CDR3 of the heavy chain and, on the other side, by the CDR1 of the light chain. Analysis of 7C8 in complex with molecular models of monomeric and trimeric gp125 highlights the importance of a conserved stretch of residues FHSQ that is localized centrally on the V3 region of gp125. Furthermore, modeling also indicates that the Fab fragment neutralizes the virus by sterically impairing subsequent engagement of the gp125 trimer with the co-receptor on the target cell.

Sidansvarig: Webbredaktion|Sidan uppdaterades: 2012-09-11
Dela:

På Göteborgs universitet använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.  Vad är kakor?