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Secondary Ligands Enhance Affinity at a Designed Metal-binding Site by Stephen F Marino; Lynne Regan is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Secondary Ligands Enhance Affinity at a Designed Metal-binding Site about?
Background: Specific interactions of metal ions with proteins are central to all life processes. The varied functions enabled by this cooperation are a consequence of strict control of the binding-site environment, particularly the number, type and geometry of metal-coordinating sidechains. Attempts to mimic these characteristics in the de nova design of metal-binding sites have thus far concentrated primarily on metal recruitment and not on affecting site function through systematic fine-tuning of the metal environment. Results: A designed tetrahedral Zn(ll)-binding site in a variant of the Bl domain of IgG-binding protein G has been expanded by introducing 'secondary ligands'. These interactions were engineered to stabilize the positions of the metal-coordinating histidine residues while retaining the desired coordination geometry. Each mutation increased the protein's affinity for metal, and combining two secondary ligands demonstrated that these enhancements are additive. These results mimic the effects of altering similar interactions observed in the native Zn(ll)-binding site of carbonic anhydrase. In the Bl system, this enhanced affinity for metal is observed despite a subst
Who reads Secondary Ligands Enhance Affinity at a Designed Metal-binding Site?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Stephen F Marino; Lynne Regan
- Publisher
- Elsevier Science; Elsevier ; Cell Press; Elsevier BV (ISSN 1074-5521)
- Published
- 1999
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)