1JBI

NMR structure of the LCCL domain

1JBI の概要

• エントリーDOI: 10.2210/pdb1jbi/pdb
• NMR情報: BMRB: 5047
• 分子名称: cochlin (1 entity in total)
• 機能のキーワード: alpha-beta protein, structural genomics, unknown function
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: O43405
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10609.98

構造登録者

Liepinsh, E.,Trexler, M.,Kaikkonen, A.,Weigelt, J.,Banyai, L.,Patthy, L.,Otting, G. (登録日: 2001-06-05, 公開日: 2001-10-17, 最終更新日: 2024-10-30)

主引用文献

Liepinsh, E.,Trexler, M.,Kaikkonen, A.,Weigelt, J.,Banyai, L.,Patthy, L.,Otting, G.
NMR structure of the LCCL domain and implications for DFNA9 deafness disorder.
EMBO J., 20:5347-5353, 2001

PubMed Abstract: The LCCL domain is a recently discovered, conserved protein module named after its presence in Limulus factor C, cochlear protein Coch-5b2 and late gestation lung protein Lgl1. The LCCL domain plays a key role in the autosomal dominant human deafness disorder DFNA9. Here we report the nuclear magnetic resonance (NMR) structure of the LCCL domain from human Coch-5b2, where dominant mutations leading to DFNA9 deafness disorder have been identified. The fold is novel. Four of the five known DFNA9 mutations are shown to involve at least partially solvent-exposed residues. Except for the Trp91Arg mutant, expression of these four LCCL mutants resulted in misfolded proteins. These results suggest that Trp91 participates in the interaction with a binding partner. The unexpected sensitivity of the fold with respect to mutations of solvent-accessible residues might be attributed to interference with the folding pathway of this disulfide-containing domain.

PubMed: 11574466
DOI: 10.1093/emboj/20.19.5347

実験手法

SOLUTION NMR