6m5y: Difference between revisions

Latest revision as of 15:18, 29 November 2023

Structure of human galectin-1 tandem-repeat mutant with lactose

Structural highlights

6m5y is a 1 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 1.38Å
Ligands:	BGC, GAL, GLC, PRD_900004, PRD_900008
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

Modification of the domain architecture of galectins has been attempted to analyze their biological functions and to develop medical applications. Several types of galectin-1 repeat mutants were previously reported but, however, it was not clear whether the native structure of the wild type was retained. In this study, we determined the crystal structure of a galectin-1 tandem-repeat mutant with a short linker peptide, and compared the unfolding profiles of the wild type and mutant by chemical denaturation. The structure of the mutant was consistent with that of the dimer of the wild type, and both carbohydrate-binding sites were retained. The unfolding curve of the wild type with lactose suggested that the dimer dissociation and the tertiary structure unfolding was concomitant at micromolar protein concentrations. The midpoint denaturant concentration of the wild type was dependent on the protein concentration and lower than that of the mutant. Linking the two subunits significantly stabilized the tertiary structure. The mutant exhibited higher T-cell growth-inhibition activity and comparable hemagglutinating activity. Structural stabilization may prevent the oxidation of the internal cysteine residue.

Crystal structure and conformational stability of a galectin-1 tandem-repeat mutant with a short linker.,Nonaka Y, Ogawa T, Shoji H, Nishi N, Kamitori S, Nakamura T Glycobiology. 2021 Oct 27. pii: 6411845. doi: 10.1093/glycob/cwab101. PMID:34735570^[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
↑ Nonaka Y, Ogawa T, Shoji H, Nishi N, Kamitori S, Nakamura T. Crystal structure and conformational stability of a galectin-1 tandem-repeat mutant with a short linker. Glycobiology. 2021 Oct 27. pii: 6411845. doi: 10.1093/glycob/cwab101. PMID:34735570 doi:https://dx.doi.org/10.1093/glycob/cwab101

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] Nonaka Y, Ogawa T, Shoji H, Nishi N, Kamitori S, Nakamura T. Crystal structure and conformational stability of a galectin-1 tandem-repeat mutant with a short linker. Glycobiology. 2021 Oct 27. pii: 6411845. doi: 10.1093/glycob/cwab101. PMID:34735570 doi:https://dx.doi.org/10.1093/glycob/cwab101

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[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='6m5y' size='340' side='right'caption='[[6m5y]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6m5y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M5Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6m5y]] is a 1 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=6M5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M5Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 1.38&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</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=6m5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m5y OCA], [https://pdbe.org/6m5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m5y RCSB], [https://www.ebi.ac.uk/pdbsum/6m5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m5y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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 26: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Kamitori, S]]
+[[Category: Kamitori S]]
-[[Category: Nakamura, T]]
+[[Category: Nakamura T]]
-[[Category: Nonaka, Y]]
+[[Category: Nonaka Y]]
-[[Category: Apoptosis]]
-[[Category: Beta-sandwich]]
-[[Category: Immune regulation]]
-[[Category: Lectin]]
-[[Category: Sugar binding protein]]

6m5y: Difference between revisions

Latest revision as of 15:18, 29 November 2023

Structure of human galectin-1 tandem-repeat mutant with lactose

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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