2H2M

Solution Structure of the N-terminal domain of COMMD1 (Murr1)

2H2M の概要

• エントリーDOI: 10.2210/pdb2h2m/pdb
• 分子名称: COMM domain-containing protein 1 (1 entity in total)
• 機能のキーワード: all alpha-helical, metal transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q8N668
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11910.60

構造登録者

Sommerhalter, M.,Zhang, Y.,Rosenzweig, A.C. (登録日: 2006-05-19, 公開日: 2006-12-05, 最終更新日: 2024-05-29)

主引用文献

Sommerhalter, M.,Zhang, Y.,Rosenzweig, A.C.
Solution Structure of the COMMD1 N-terminal Domain.
J.Mol.Biol., 365:715-721, 2007

PubMed Abstract: COMMD1 is the prototype of a new protein family that plays a role in several important cellular processes, including NF-kappaB signaling, sodium transport, and copper metabolism. The COMMD proteins interact with one another via a conserved C-terminal domain, whereas distinct functions are predicted to result from a variable N-terminal domain. The COMMD proteins have not been characterized biochemically or structurally. Here, we present the solution structure of the N-terminal domain of COMMD1 (N-COMMD1, residues 1-108). This domain adopts an alpha-helical structure that bears little resemblance to any other helical protein. The compact nature of N-COMMD1 suggests that full-length COMMD proteins are modular, consistent with specific functional properties for each domain. Interactions between N-COMMD1 and partner proteins may occur via complementary electrostatic surfaces. These data provide a new foundation for biochemical characterization of COMMD proteins and for probing COMMD1 protein-protein interactions at the molecular level.

PubMed: 17097678
DOI: 10.1016/j.jmb.2006.10.030

実験手法

SOLUTION NMR