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Selected Publication:

Gach, JS; Furtmüller, PG; Quendler, H; Messner, P; Wagner, R; Katinger, H; Kunert, R.
(2010): Proline is not uniquely capable of providing the pivot point for domain swapping in 2G12, a broadly neutralizing antibody against HIV-1.
J Biol Chem. 2010; 285(2):1122-1127 FullText FullText_BOKU

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.
Authors BOKU Wien:
Furtmüller Paul Georg
Katinger Hermann
Kunert Renate
Messner Paul
Quendler Heribert
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Animals -
Antibodies, Monoclonal - chemistry
Antibodies, Neutralizing - chemistry
Antibodies, Viral - chemistry
CHO Cells -
Cricetinae -
Cricetulus -
HIV Envelope Protein gp120 - chemistry
HIV-1 - chemistry
Humans -
Proline - chemistry
Protein Structure, Tertiary -

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