This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4xbl

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

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

Structural highlights

4xbl is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.931Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEG1_HUMAN May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.^[1] ^[2]

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^[3]

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

References

↑ He J, Baum LG. Presentation of galectin-1 by extracellular matrix triggers T cell death. J Biol Chem. 2004 Feb 6;279(6):4705-12. Epub 2003 Nov 14. PMID:14617626 doi:10.1074/jbc.M311183200
↑ Nishi N, Abe A, Iwaki J, Yoshida H, Itoh A, Shoji H, Kamitori S, Hirabayashi J, Nakamura T. Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. Glycobiology. 2008 Dec;18(12):1065-73. Epub 2008 Sep 16. PMID:18796645 doi:10.1093/glycob/cwn089
↑ 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 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Homo sapiens | Large Structures | Hsieh TJ | Lin CH | Lin HY

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Human Galectin-1 in Complex with Type 1 N-acetyllactosamine==
-<StructureSection load='4xbl' size='340' side='right' caption='[[4xbl]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
+<StructureSection load='4xbl' size='340' side='right'caption='[[4xbl]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4xbl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XBL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XBL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4xbl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XBL FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.931&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <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">[[4xbn|4xbn]], [[4xbq|4xbq]]</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=4xbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xbl OCA], [https://pdbe.org/4xbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xbl RCSB], [https://www.ebi.ac.uk/pdbsum/4xbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xbl ProSAT]</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=4xbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xbl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xbl RCSB], [http://www.ebi.ac.uk/pdbsum/4xbl PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LEG1_HUMAN LEG1_HUMAN]] May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.<ref>PMID:14617626</ref> <ref>PMID:18796645</ref>
+[https://www.uniprot.org/uniprot/LEG1_HUMAN LEG1_HUMAN] May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.<ref>PMID:14617626</ref> <ref>PMID:18796645</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4xbl" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Galectin 3D structures|Galectin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Hsieh, T J]]
+[[Category: Homo sapiens]]
-[[Category: Lin, C H]]
+[[Category: Large Structures]]
-[[Category: Lin, H Y]]
+[[Category: Hsieh TJ]]
-[[Category: Complex]]
+[[Category: Lin CH]]
-[[Category: Human galectin-1]]
+[[Category: Lin HY]]
-[[Category: Sugar binding protein]]
-[[Category: Type 1 lacnac]]

4xbl

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox