1no8
From Proteopedia
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SOLUTION STRUCTURE OF THE NUCLEAR FACTOR ALY RBD DOMAIN
Overview
ALY is a ubiquitously expressed nuclear protein which interacts with, proteins such as TAP that are involved in export of mRNA from the nucleus, to the cytoplasm, as well as with proteins that bind the T cell receptor, alpha gene enhancer. ALY has also been shown to bind mRNA and to, co-localize in the nucleus with components of a multiprotein postsplicing, complex that is deposited 20-24 nucleotides upstream of exon-exon, junctions. ALY has a conserved RNA binding domain (RBD) flanked by Gly-Arg, rich N-terminal and C-terminal sequences. We determined the solution, structure of the RBD homology region in ALY by nuclear magnetic resonance, methods. The RBD motif in ALY has a characteristic, beta(1)alpha(1)beta(2)-beta(3)alpha(2)beta(4) fold, consisting of a beta, sheet composed of four antiparallel beta strands and two alpha helices, that pack on one face of the beta sheet. As in other RBD structures, the, beta sheet has an exposed face with hydrophobic and charged residues that, could modulate interactions with other molecules. The loop that connects, beta strands 2 and 3 is in intermediate motion in the NMR time scale, which is also characteristic of other RBDs. This loop presents side chains, close to the exposed surface of the beta sheet and is a primary candidate, site for intermolecular interactions. The structure of the conserved RBD, of ALY provides insight into the nature of interactions involving this, multifunctional protein.
About this Structure
1NO8 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processes., Perez-Alvarado GC, Martinez-Yamout M, Allen MM, Grosschedl R, Dyson HJ, Wright PE, Biochemistry. 2003 Jun 24;42(24):7348-57. PMID:12809490
Page seeded by OCA on Tue Nov 20 22:25:31 2007
