4xbn

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(Difference between revisions)

Revision as of 01:44, 10 March 2017

Crystal Structure of Human Galectin-3 CRD in Complex with Type 1 N-acetyllactosamine

Structural highlights

4xbn is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4xbl, 4xbq
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Galectins represent beta-galactoside-binding proteins and are known to bind Galbeta1-3/4GlcNAc disaccharides (abbreviated as LN1 and LN2, respectively). Despite high sequence and structural homology shared by the carbohydrate recognition domain (CRD) of all galectin members, how each galectin displays different sugar-binding specificity still remains ambiguous. Herein we provided the first structural evidence of human galectins-1, 3-CRD and 7 in complex with LN1. Galectins-1 and 3 were shown to have higher affinity for LN2 than for LN1, while galectin-7 displayed the reversed specificity. In comparison with the previous LN2-complexed structures, the results indicated that the average glycosidic torsion angle of galectin-bound LN1 (psiLN1 approximately 135 degrees ) was significantly differed from that of galectin-bound LN2 (psiLN2 approximately -108 degrees ), i.e. the GlcNAc moiety adopted a different orientation to maintain essential interactions. Furthermore, we also identified an Arg-Asp/Glu-Glu-Arg salt-bridge network and the corresponding loop (to position the second Asp/Glu residue) critical for the LN1/2-binding preference.

Structural Basis Underlying the Binding Preference of Human Galectins-1, -3 and -7 for Galbeta1-3/4GlcNAc.,Hsieh TJ, Lin HY, Tu Z, Huang BS, Wu SC, Lin CH PLoS One. 2015 May 6;10(5):e0125946. doi: 10.1371/journal.pone.0125946., eCollection 2015. PMID:25945972^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fukushi J, Makagiansar IT, Stallcup WB. NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin. Mol Biol Cell. 2004 Aug;15(8):3580-90. Epub 2004 Jun 4. PMID:15181153 doi:http://dx.doi.org/10.1091/mbc.E04-03-0236
↑ Henderson NC, Sethi T. The regulation of inflammation by galectin-3. Immunol Rev. 2009 Jul;230(1):160-71. doi: 10.1111/j.1600-065X.2009.00794.x. PMID:19594635 doi:10.1111/j.1600-065X.2009.00794.x
↑ Haudek KC, Spronk KJ, Voss PG, Patterson RJ, Wang JL, Arnoys EJ. Dynamics of galectin-3 in the nucleus and cytoplasm. Biochim Biophys Acta. 2010 Feb;1800(2):181-189. Epub 2009 Jul 16. PMID:19616076 doi:S0304-4165(09)00194-9
↑ Hsieh TJ, Lin HY, Tu Z, Huang BS, Wu SC, Lin CH. Structural Basis Underlying the Binding Preference of Human Galectins-1, -3 and -7 for Galbeta1-3/4GlcNAc. PLoS One. 2015 May 6;10(5):e0125946. doi: 10.1371/journal.pone.0125946., eCollection 2015. PMID:25945972 doi:http://dx.doi.org/10.1371/journal.pone.0125946

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xbn"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Human Galectin-3 CRD in Complex with Type 1 N-acetyllactosamine==
 <StructureSection load='4xbn' size='340' side='right' caption='[[4xbn]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xbl|4xbl]], [[4xbq|4xbq]]</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=4xbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xbn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xbn RCSB], [http://www.ebi.ac.uk/pdbsum/4xbn PDBsum]</span></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=4xbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xbn OCA], [http://pdbe.org/4xbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xbn RCSB], [http://www.ebi.ac.uk/pdbsum/4xbn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xbn ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4xbn" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4xbn

From Proteopedia

Revision as of 01:44, 10 March 2017

Crystal Structure of Human Galectin-3 CRD in Complex with Type 1 N-acetyllactosamine

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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