Gach, Johannes S. and Furtmueller, Paul G. and Quendler, Heribert and Messner, Paul and Wagner, Ralf and Katinger, Hermann and Kunert, Renate (2010) Proline Is Not Uniquely Capable of Providing the Pivot Point for Domain Swapping in 2G12, a Broadly Neutralizing Antibody against HIV-1. JOURNAL OF BIOLOGICAL CHEMISTRY, 285 (2). pp. 1122-1127. ISSN 0021-9258,
Full text not available from this repository. (Request a copy)Abstract
The human monoclonal antibody 2G12 is a member of a small group of broadly neutralizing antibodies against human immunodeficiency virus type 1. 2G12 adopts a unique variable heavy domain-exchanged dimeric configuration that results in an extensive multivalent binding surface and the ability to bind with high affinity to densely clustered high mannose oligosaccharides on the "silent" face of the gp120 envelope glycoprotein. Here, we further define the amino acids responsible for this extraordinary domain-swapping event in 2G12.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | IMMUNODEFICIENCY-VIRUS TYPE-1; ANTIIDIOTYPIC ANTIBODY; 2F5; RECOGNITION; FRAGMENT; VACCINE; BINDING; REGION; GP120; LEVEL; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 10 Aug 2020 09:10 |
| Last Modified: | 10 Aug 2020 09:10 |
| URI: | https://pred.uni-regensburg.de/id/eprint/25316 |
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