1ZIK

GCN4-LEUCINE ZIPPER CORE MUTANT ASN16LYS IN THE DIMERIC STATE

1ZIK の概要

• エントリーDOI: 10.2210/pdb1zik/pdb
• 分子名称: GENERAL CONTROL PROTEIN GCN4 (2 entities in total)
• 機能のキーワード: leucine zipper, amino-acid biosynthesis, transcription regulation, activator, dna-binding, nuclear protein, coiled coil
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P03069
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8041.48

構造登録者

Gonzalez Junior, L.,Woolfson, D.N.,Alber, T. (登録日: 1996-10-30, 公開日: 1997-07-07, 最終更新日: 2024-02-14)

主引用文献

Gonzalez Jr., L.,Woolfson, D.N.,Alber, T.
Buried polar residues and structural specificity in the GCN4 leucine zipper.
Nat.Struct.Biol., 3:1011-1018, 1996

PubMed Abstract: A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine zipper selectively favours the parallel, dimeric, coiled-coil structure. To test if other polar residues confer oligomerization specificity, the structural effects of Gln and Lys substitutions for Asn 16 were characterized. Like the wild-type peptide, the Asn 16Lys mutant formed exclusively dimers. In contrast, Gln 16, despite its chemical similarity to Asn, allowed the peptide to form both dimers and trimers. The Gln 16 side chain was accommodated by qualitatively different interactions in the dimer and trimer crystal structures. These findings demonstrate that the structural selectivity of polar residues results not only from the burial of polar atoms, but also depends on the complementarity of the side-chain stereochemistry with the surrounding structural environment.

PubMed: 8946854
DOI: 10.1038/nsb1296-1011

実験手法

X-RAY DIFFRACTION (1.8 Å)