2u1a
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(New page: 200px<br /> <applet load="2u1a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2u1a" /> '''RNA BINDING DOMAIN 2 OF HUMAN U1A PROTEIN, ...)
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Revision as of 21:32, 12 November 2007
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RNA BINDING DOMAIN 2 OF HUMAN U1A PROTEIN, NMR, 20 STRUCTURES
Overview
The human U1A protein has two putative RNA binding domains, one at the, N-terminal region of the protein (RBD1) and the other at the C-terminal, end (RBD2). RBD1 binds tightly and specifically to one of the stem loops, of the U1 snRNA, as well as to its own 3'-UTR. In contrast, RBD2 does not, appear to associate with any RNA. The two domains share 25% amino acid, identity, and both have the same betaalphabeta-betaalphabeta secondary, structure fold. In this work, 13C/15N/1H multidimensional NMR methods were, used to obtain side-chain assignments for RBD2, and then the tertiary, structure was calculated using a distance geometry/simulated annealing, algorithm that employs pairwise Gaussian metrization. RBD2 is shown to, fold into an alpha/beta sandwich with a four-stranded antiparallel, beta-sheet, which is the typical global topology of these domains., Specific structural features of RBD2 include a beta-bulge in beta2, N-capping boxes for both alpha-helices, and an extremely shallow twist of, its beta-sheet. The 15N backbone dynamics of these two structurally, homologous RBDs are significantly different, compared using order, parameters and T2 exchange terms in the Lipari and Szabo model-free, formalism. Conformational exchange observed in RBD1, which is absent in, RBD2, may correlate to the mechanism of RNA binding.
About this Structure
2U1A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the human U1A protein determined by NMR spectroscopy., Lu J, Hall KB, Biochemistry. 1997 Aug 26;36(34):10393-405. PMID:9265619
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