Structural highlights
Function
[SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gbeta1m2 suggests that the increased stability of Gbeta1m2 is due to increased helix propensity and more favorable helix dipole interactions.
Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design.,Strop P, Marinescu AM, Mayo SL Protein Sci. 2000 Jul;9(7):1391-4. PMID:10933505[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Strop P, Marinescu AM, Mayo SL. Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design. Protein Sci. 2000 Jul;9(7):1391-4. PMID:10933505
