2kiv | pdb_00002kiv

AIDA-1 SAM domain tandem

spinqualitylabelsall models 2kiv, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kiv is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: AIDA-1b, ANKS1B (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ANS1B_HUMAN] Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells. Isoform 3 can regulate global protein synthesis by altering nucleolar numbers (By similarity). Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import.,Kurabi A, Brener S, Mobli M, Kwan JJ, Donaldson LW J Mol Biol. 2009 Oct 9;392(5):1168-77. Epub 2009 Aug 8. PMID:19666031 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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