One-step evolution of a dimer from a monomeric protein

Autor:	Apostolos G. Gittis, Alan K. Meeker, Eaton E. Lattman, Susan M. Green
Rok vydání:	1995
Předmět:	chemistry.chemical_classification Stereochemistry Dimer One-Step Crystal structure Amino acid chemistry.chemical_compound Crystallography Monomer chemistry Structural Biology Normal position Hydrolase Molecular Biology Staphylococcal Nuclease
Zdroj:	Nature Structural & Molecular Biology. 2:746-751
ISSN:	1545-9985 1545-9993
DOI:	10.1038/nsb0995-746
Popis:	Deletion of six amino acids in a surface loop transforms staphylococcal nuclease from a monomeric protein into a very stable dimer (Kd < 1 x 10(-8)M). A 2 A X-ray crystal structure of the dimer (R = 0.176) shows that the carboxy-terminal alpha-helix has been stripped from its normal position in one monomer and is now incorporated into the equivalent position on the adjoining monomer. This swapping creates an association interface of 2900 A 2. A second, smaller interface of 460 A 2 is also formed. The spontaneous exchange or swapping of secondary structural elements provides a simple pathway for the formation of large, stable protein/protein interfaces and may play an important role in the evolution of oligomeric proteins.
Databáze:	OpenAIRE
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