5fx0: Difference between revisions
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The | ==Fasciola hepatica calcium binding protein FhCaBP2: Structure of the dynein light chain-like domain. P6422 native.== | ||
<StructureSection load='5fx0' size='340' side='right' caption='[[5fx0]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fx0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FX0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FX0 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fwz|5fwz]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fx0 OCA], [http://pdbe.org/5fx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fx0 RCSB], [http://www.ebi.ac.uk/pdbsum/5fx0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The common liver fluke Fasciola hepatica causes an increasing burden on human and animal health, partly because of the spread of drug-resistant isolates. As a consequence, there is considerable interest in developing new drugs to combat liver fluke infections. A group of potential targets is a family of calcium-binding proteins which combine an N-terminal domain with two EF-hand motifs and a C-terminal domain with predicted similarity to dynein light chains (DLC-like domain). The function of these proteins is unknown, although in several species, they have been localised to the tegument, an important structure at the host-parasite interface. Here, we report the X-ray crystal structure of the DLC-like domain of F. hepatica calcium-binding protein 2 (FhCaBP2), solved using single-wavelength anomalous diffraction and refined at 2.3 A resolution in two different crystal forms. The FhCaBP2 DLC-like domain has a structure similar to other DLC domains, with an anti-parallel beta-sheet packed against an alpha-helical hairpin. Like other DLC domains, it dimerises through its beta2-strand, which extends in an arch and forms the fifth strand in an extended beta-sheet of the other monomer. The structure provides molecular details of the dimerisation of FhCaBP2, the first example from this family of parasite proteins. | |||
Fasciola hepatica calcium-binding protein FhCaBP2: structure of the dynein light chain-like domain.,Nguyen TH, Thomas CM, Timson DJ, van Raaij MJ Parasitol Res. 2016 Apr 16. PMID:27083189<ref>PMID:27083189</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5fx0" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Nguyen, T H]] | |||
[[Category: Raaij, M J.van]] | |||
[[Category: Thomas, C M]] | |||
[[Category: Timson, D J]] | |||
[[Category: Cell adhesion]] | |||
