3R8B

Crystal structure of Staphylococcal Enterotoxin B in complex with an affinity matured mouse TCR VBeta8.2 protein, G5-8

Summary for 3R8B

• Entry DOI: 10.2210/pdb3r8b/pdb
• Descriptor: Enterotoxin type B, G5-8, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: immunoglobulin-like, ob-fold, toxin-immune system complex, toxin/immune system
• Biological source: Staphylococcus aureus; More
• Cellular location: Secreted: P01552
• Total number of polymer chains: 16
• Total formula weight: 340022.96

Authors

Bonsor, D.A.,Sundberg, E.J. (deposition date: 2011-03-23, release date: 2011-04-06, Last modification date: 2024-10-16)

Primary citation

Bonsor, D.A.,Postel, S.,Pierce, B.G.,Wang, N.,Zhu, P.,Buonpane, R.A.,Weng, Z.,Kranz, D.M.,Sundberg, E.J.
Molecular basis of a million-fold affinity maturation process in a protein-protein interaction.
J.Mol.Biol., 411:321-328, 2011

PubMed Abstract: Protein engineering is becoming increasingly important for pharmaceutical applications where controlling the specificity and affinity of engineered proteins is required to create targeted protein therapeutics. Affinity increases of several thousand-fold are now routine for a variety of protein engineering approaches, and the structural and energetic bases of affinity maturation have been investigated in a number of such cases. Previously, a 3-million-fold affinity maturation process was achieved in a protein-protein interaction composed of a variant T-cell receptor fragment and a bacterial superantigen. Here, we present the molecular basis of this affinity increase. Using X-ray crystallography, shotgun reversion/replacement scanning mutagenesis, and computational analysis, we describe, in molecular detail, a process by which extrainterfacial regions of a protein complex can be rationally manipulated to significantly improve protein engineering outcomes.

PubMed: 21689661
DOI: 10.1016/j.jmb.2011.06.009

Experimental method

X-RAY DIFFRACTION (2.95 Å)