View source for 6fof


==Crystal structure of a crystallized variant of h-Gal3: Gal-3[NTS/VII-IX]==
<StructureSection load='6fof' size='340' side='right' caption='[[6fof]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fof]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FOF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6fof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fof OCA], [http://pdbe.org/6fof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fof RCSB], [http://www.ebi.ac.uk/pdbsum/6fof PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fof ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/LEG3_HUMAN LEG3_HUMAN]] Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells.<ref>PMID:15181153</ref> <ref>PMID:19594635</ref> <ref>PMID:19616076</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Among members of the family of adhesion/growth-regulatory galectins, galectin-3 (Gal-3) bears a unique modular architecture. A N-terminal tail (NT) consisting of the N-terminal segment (NTS) and nine collagen-like repeats is linked to the canonical lectin domain. In contrast to bivalent proto- and tandem-repeat-type galectins, Gal-3 is monomeric in solution, capable to self-associate in the presence of bi- to multivalent ligands, and the NTS is involved in cellular compartmentalization. Since no crystallographic information on Gal-3 beyond the lectin domain is available, we used a shortened variant with NTS and repeats VII-IX. This protein crystallized as tetramers with contacts between the lectin domains. The region from Tyr101 (in repeat IX) to Leu114 (in the CRD) formed a hairpin. The NTS extends the canonical beta-sheet of F1-F5 strands with two new beta-strands on the F face. Together, crystallographic and SAXS data reveal a mode of intramolecular structure building involving the highly flexible Gal-3's NT.

Crystallization of a human galectin-3 variant with two ordered segments in the shortened N-terminal tail.,Flores-Ibarra A, Vertesy S, Medrano FJ, Gabius HJ, Romero A Sci Rep. 2018 Jun 29;8(1):9835. doi: 10.1038/s41598-018-28235-x. PMID:29959397<ref>PMID:29959397</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fof" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Flores-Ibarra, A]]
[[Category: Medrano, F J]]
[[Category: Romero, A]]
[[Category: Apoptosis]]
[[Category: Galectin]]
[[Category: Glycosylation]]
[[Category: Sugar binding protein]]