Structural highlights
Function
[RARC_BPP22] This protein acts as a transcriptional repressor of its own gene arc and of gene ant.
Publication Abstract from PubMed
The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic residues in combinatorial randomization experiments resulting in active mutants that are significantly more stable than wild type. The crystal structure of one mutant reveals that the mutant side chains pack against each other in an otherwise wild-type fold. Thus, simple hydrophobic interactions provide more stabilizing energy than the buried salt bridge and confer comparable conformational specificity.
Are buried salt bridges important for protein stability and conformational specificity?,Waldburger CD, Schildbach JF, Sauer RT Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:7749916[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Waldburger CD, Schildbach JF, Sauer RT. Are buried salt bridges important for protein stability and conformational specificity? Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:7749916
