3wuc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==X-ray crystal structure of Xenopus laevis galectin-Va== | ==X-ray crystal structure of Xenopus laevis galectin-Va== | ||
<StructureSection load='3wuc' size='340' side='right'caption='[[3wuc]]' scene=''> | <StructureSection load='3wuc' size='340' side='right'caption='[[3wuc]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WUC FirstGlance]. <br> | <table><tr><td colspan='2'>[[3wuc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WUC 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=3wuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wuc OCA], [https://pdbe.org/3wuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wuc RCSB], [https://www.ebi.ac.uk/pdbsum/3wuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wuc ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PRD_900008:alpha-lactose'>PRD_900008</scene></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=3wuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wuc OCA], [https://pdbe.org/3wuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wuc RCSB], [https://www.ebi.ac.uk/pdbsum/3wuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wuc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q91786_XENLA Q91786_XENLA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Xenopus laevis (African clawed frog) has two types of proto-type galectins that are similar to mammalian galectin-1 in amino acid sequence. One type, comprising xgalectin-Ia and -Ib, is regarded as being equivalent to galectin-1, and the other type, comprising xgalectin-Va and -Vb, is expected to be a unique galectin subgroup. The latter is considerably abundant in frog skin, however, its biological function remains unclear. We determined the crystal structures of two proto-type galectins, xgalectin-Ib and -Va. The structures showed that both galectins formed a mammalian galectin-1-like homodimer, and furthermore, xgalectin-Va formed a homotetramer. This tetramer structure has not been reported for other galectins. Gel filtration and other experiments indicated that xgalectin-Va was in a dimer-tetramer equilibrium in solution, and lactose binding enhanced the tetramer formation. The residues involved in the dimer-dimer association were conserved in xgalectin-Va and -Vb, and one of the Xenopus (Silurana) tropicalis proto-type galectins, but not in xgalectin-Ia and -Ib, and other galectin-1-equivalent proteins. Xgalectin-Va preferred Galbeta1-3GalNAc and not Galbeta1-4GlcNAc, while xgalectin-Ib preferred Galbeta1-4GlcNAc as well as human galectin-1. Xgalectin-Va/Vb would have diverged from the galectin-1 group with accompanying acquisition of the higher oligomer formation and altered ligand selectivity. | |||
Crystal structure of a Xenopus laevis skin proto-type galectin, close to but distinct from galectin-1.,Nonaka Y, Ogawa T, Yoshida H, Shoji H, Nishi N, Kamitori S, Nakamura T Glycobiology. 2015 Mar 24. pii: cwv020. PMID:25804418<ref>PMID:25804418</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wuc" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Galectin 3D structures|Galectin 3D structures]] | *[[Galectin 3D structures|Galectin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Xenopus laevis]] | |||
[[Category: Kamitori S]] | [[Category: Kamitori S]] | ||
[[Category: Nakamura T]] | [[Category: Nakamura T]] | ||
[[Category: Nonaka Y]] | [[Category: Nonaka Y]] | ||
[[Category: Yoshida H]] | [[Category: Yoshida H]] | ||
Latest revision as of 16:29, 8 November 2023
X-ray crystal structure of Xenopus laevis galectin-VaX-ray crystal structure of Xenopus laevis galectin-Va
Structural highlights
FunctionPublication Abstract from PubMedXenopus laevis (African clawed frog) has two types of proto-type galectins that are similar to mammalian galectin-1 in amino acid sequence. One type, comprising xgalectin-Ia and -Ib, is regarded as being equivalent to galectin-1, and the other type, comprising xgalectin-Va and -Vb, is expected to be a unique galectin subgroup. The latter is considerably abundant in frog skin, however, its biological function remains unclear. We determined the crystal structures of two proto-type galectins, xgalectin-Ib and -Va. The structures showed that both galectins formed a mammalian galectin-1-like homodimer, and furthermore, xgalectin-Va formed a homotetramer. This tetramer structure has not been reported for other galectins. Gel filtration and other experiments indicated that xgalectin-Va was in a dimer-tetramer equilibrium in solution, and lactose binding enhanced the tetramer formation. The residues involved in the dimer-dimer association were conserved in xgalectin-Va and -Vb, and one of the Xenopus (Silurana) tropicalis proto-type galectins, but not in xgalectin-Ia and -Ib, and other galectin-1-equivalent proteins. Xgalectin-Va preferred Galbeta1-3GalNAc and not Galbeta1-4GlcNAc, while xgalectin-Ib preferred Galbeta1-4GlcNAc as well as human galectin-1. Xgalectin-Va/Vb would have diverged from the galectin-1 group with accompanying acquisition of the higher oligomer formation and altered ligand selectivity. Crystal structure of a Xenopus laevis skin proto-type galectin, close to but distinct from galectin-1.,Nonaka Y, Ogawa T, Yoshida H, Shoji H, Nishi N, Kamitori S, Nakamura T Glycobiology. 2015 Mar 24. pii: cwv020. PMID:25804418[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||