2KIV

AIDA-1 SAM domain tandem

2KIV の概要

• エントリーDOI: 10.2210/pdb2kiv/pdb
• NMR情報: BMRB: 16297
• 分子名称: Ankyrin repeat and sterile alpha motif domain-containing protein 1B (1 entity in total)
• 機能のキーワード: sam domain, tandem, signaling protein, alternative splicing, ank repeat, cell junction, cell membrane, cell projection, cytoplasm, membrane, nucleus, phosphoprotein, postsynaptic cell membrane, synapse
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16672.16

構造登録者

Donaldson, L.W.,Kurabi, A. (登録日: 2009-05-12, 公開日: 2009-08-25, 最終更新日: 2024-05-08)

主引用文献

Kurabi, A.,Brener, S.,Mobli, M.,Kwan, J.J.,Donaldson, L.W.
A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import.
J.Mol.Biol., 392:1168-1177, 2009

PubMed Abstract: The neuronal scaffolding protein AIDA-1 is believed to act as a convener of signals arising at postsynaptic densities. Among the readily identifiable domains in AIDA-1, two closely juxtaposed sterile alpha motif (SAM) domains and a phosphotyrosine binding domain are located within the C-terminus of the longest splice variant and exclusively in four shorter splice variants. As a first step towards understanding the possible emergent properties arising from this assembly of ligand binding domains, we have used NMR methods to solve the first structure of a SAM domain tandem. Separated by a 15-aa linker, the two SAM domains are fused in a head-to-tail orientation that has been observed in other hetero- and homotypic SAM domain structures. The basic nuclear import signal for AIDA-1 is buried at the interface between the two SAM domains. An observed disparity between the thermal stabilities of the two SAM domains suggests a mechanism whereby the second SAM domain decouples from the first SAM domain to facilitate translocation of AIDA-1 to the nucleus.

PubMed: 19666031
DOI: 10.1016/j.jmb.2009.08.004

実験手法

SOLUTION NMR