2KIV
AIDA-1 SAM domain tandem
Summary for 2KIV
| Entry DOI | 10.2210/pdb2kiv/pdb |
| NMR Information | BMRB: 16297 |
| Descriptor | Ankyrin repeat and sterile alpha motif domain-containing protein 1B (1 entity in total) |
| Functional Keywords | sam domain, tandem, signaling protein, alternative splicing, ank repeat, cell junction, cell membrane, cell projection, cytoplasm, membrane, nucleus, phosphoprotein, postsynaptic cell membrane, synapse |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 16672.16 |
| Authors | Donaldson, L.W.,Kurabi, A. (deposition date: 2009-05-12, release date: 2009-08-25, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 19666031DOI: 10.1016/j.jmb.2009.08.004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
