PDBsum entry 2kiv

Signaling protein

PDB id: 2kiv

Contents

Protein chain

135 a.a. *

* Residue conservation analysis

PDB id:

2kiv

Name:

Signaling protein

Title:

Aida-1 sam domain tandem

Structure:

Ankyrin repeat and sterile alpha motif domain-containing protein 1b. Chain: a. Fragment: sam1 and sam2 domains. Synonym: amyloid-beta protein intracellular domain-associated protein 1, aida-1, e2a-pbx1-associated protein, eb-1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: aida-1b, anks1b. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: bl21:de3.

NMR struc:

20 models

Authors:

L.W.Donaldson,A.Kurabi

Key ref:

A.Kurabi et al. (2009). 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. PubMed id: 19666031 DOI: 10.1016/j.jmb.2009.08.004

Date:

12-May-09 Release date: 25-Aug-09

Protein chain

Q7Z6G8  (ANS1B_HUMAN) -  Ankyrin repeat and sterile alpha motif domain-containing protein 1B from Homo sapiens

Seq: 1248 a.a.

Struc: 135 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/j.jmb.2009.08.004

J Mol Biol 392:1168-1177 (2009)

PubMed id: 19666031

A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import.

A.Kurabi, S.Brener, M.Mobli, J.J.Kwan, L.W.Donaldson.

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.

Selected figure(s)

Figure 4.
Fig. 4. Effect of linker length on the orientation of the SAM1 and SAM2 domains in the tandem. Protein structures were solved using experimental data that had been transposed in sequence number to reflect a successively shortened linker. The RMSD difference between each linker variant and the wild-type structure (length = 15) plotted against linker length.

Figure 7.
Fig. 7. A diverse array of SAM domain partnerships. The Ephrin kinase SAM domains have been crystallized in Head–Head (involving helix 1) and Tail–Tail orientations (involving helix 5). The Head–Tail orientation to which the AIDA-1 SAM tandem belongs is shared with the heterotypic SAM partnerships of human/Drosophila CNK2/HYP, Drosophila Ph/Scm, and S. cerevisiae Ste11/Ste50, among others. PDB codes of the relevant structures are indicated.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2009, 392, 1168-1177) copyright 2009.

Figures were selected by an automated process.