1xbs

<table><tr><td colspan='2'>[[1xbs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XBS FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xbs OCA], [https://pdbe.org/1xbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xbs RCSB], [https://www.ebi.ac.uk/pdbsum/1xbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xbs ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The U4/U6*U5 tri-snRNP complex is the catalytic core of the pre-mRNA splicing machinery. The thioredoxin-like protein hDim1 (U5-15 kDa) constitutes an essential component of the U5 particle, and its functions have been reported to be highly conserved throughout evolution. Recently, the Dim1-like protein (DLP) family has been extended to other proteins harboring similar sequence motifs. Here we report the biochemical characterization and crystallographic structure of a 149 amino acid protein, hDim2, which shares 38% sequence identity with hDim1. The crystallographic structure of hDim2 solved at 2.5 A reveals a classical thioredoxin-fold structure. However, despite the similarity in the thioredoxin fold, hDim2 differs from hDim1 in many significant features. The structure of hDim2 contains an extra alpha helix (alpha3) and a beta strand (beta5), which stabilize the protein, suggesting that they may be involved in interactions with hDim2-specific partners. The stability and thermodynamic parameters of hDim2 were evaluated by combining circular dichroism and fluorescence spectroscopy together with chromatographic and cross-linking approaches. We have demonstrated that, in contrast to hDim1, hDim2 forms stable homodimers. The dimer interface is essentially stabilized by electrostatic interactions and involves tyrosine residues located in the alpha3 helix. Structural analysis reveals that hDim2 lacks some of the essential structural motifs and residues that are required for the biological activity and interactive properties of hDim1. Therefore, on the basis of structural investigations we suggest that, in higher eukaryotes, although both hDim1 and hDim2 are involved in pre-mRNA splicing, the two proteins are likely to participate in different multisubunit complexes and biological processes.

Biochemical characterization and crystal structure of a Dim1 family associated protein: Dim2.,Simeoni F, Arvai A, Bello P, Gondeau C, Hopfner KP, Neyroz P, Heitz F, Tainer J, Divita G Biochemistry. 2005 Sep 13;44(36):11997-2008. PMID:16142897<ref>PMID:16142897</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1xbs" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Arvai, A]]

[[Category: Bello, P]]

[[Category: Divita, G]]

[[Category: Gondeau, C]]

[[Category: Heitz, F]]

[[Category: Hopfner, K P]]

[[Category: Simeoni, F]]

[[Category: Tainer, J]]

[[Category: Transcription]]