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2km2

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Galectin-1 dimer

Structural highlights

2km2 is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Galectins are a family of lectins with a conserved carbohydrate recognition domain that interacts with beta-galactosides. By binding cell surface glycoconjugates, galectin-1 (gal-1) is involved in cell adhesion and migration processes and is an important regulator of tumor angiogenesis. Here, we used heteronuclear NMR spectroscopy and molecular modeling to investigate lactose binding to gal-1 and to derive solution NMR structures of gal-1 in the lactose-bound and unbound states. Structure analysis shows that the beta-strands and loops around the lactose binding site, which are more open and dynamic in the unbound state, fold in around the bound lactose molecule, dampening internal motions at that site and increasing motions elsewhere throughout the protein to contribute entropically to the binding free energy. CD data support the view of an overall more open structure in the lactose-bound state. Analysis of heteronuclear single quantum coherence titration binding data indicates that lactose binds the two carbohydrate recognition domains of the gal-1 dimer with negative cooperativity, in that the first lactose molecule binds more strongly (K(1)=21+/-6 x 10(3) M(-1)) than the second (K(2)=4+/-2 x 10(3) M(-1)). Isothermal calorimetry data fit using a sequential binding model present a similar picture, yielding K(1)=20+/-10 x 10(3) M(-1) and K(2)=1.67+/-0.07 x 10(3) M(-1). Molecular dynamics simulations provide insight into structural dynamics of the half-loaded lactose state and, together with NMR data, suggest that lactose binding at one site transmits a signal through the beta-sandwich and loops to the second binding site. Overall, our results provide new insight into gal-1 structure-function relationships and to protein-carbohydrate interactions in general.

Lactose binding to galectin-1 modulates structural dynamics, increases conformational entropy, and occurs with apparent negative cooperativity.,Nesmelova IV, Ermakova E, Daragan VA, Pang M, Menendez M, Lagartera L, Solis D, Baum LG, Mayo KH J Mol Biol. 2010 Apr 16;397(5):1209-30. Epub 2010 Feb 23. PMID:20184898^[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
↑ Nesmelova IV, Ermakova E, Daragan VA, Pang M, Menendez M, Lagartera L, Solis D, Baum LG, Mayo KH. Lactose binding to galectin-1 modulates structural dynamics, increases conformational entropy, and occurs with apparent negative cooperativity. J Mol Biol. 2010 Apr 16;397(5):1209-30. Epub 2010 Feb 23. PMID:20184898 doi:10.1016/j.jmb.2010.02.033

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2km2"

@@ Line 1: / Line 1: @@
 ==Galectin-1 dimer==
-<StructureSection load='2km2' size='340' side='right' caption='[[2km2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2km2' size='340' side='right'caption='[[2km2]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2km2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KM2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KM2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2km2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KM2 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LGALS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2km2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2km2 RCSB], [http://www.ebi.ac.uk/pdbsum/2km2 PDBsum]</span></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=2km2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2km2 OCA], [https://pdbe.org/2km2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2km2 RCSB], [https://www.ebi.ac.uk/pdbsum/2km2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2km2 ProSAT]</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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/2km2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/2km2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2km2 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2km2" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Galectin|Galectin]]
+*[[Galectin 3D structures|Galectin 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 36: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Baum, L G]]
+[[Category: Large Structures]]
-[[Category: Daragan, V A]]
+[[Category: Baum LG]]
-[[Category: Ermakova, E]]
+[[Category: Daragan VA]]
-[[Category: Mayo, K H]]
+[[Category: Ermakova E]]
-[[Category: Nesmelova, I V]]
+[[Category: Mayo KH]]
-[[Category: Pang, M]]
+[[Category: Nesmelova IV]]
-[[Category: Beta-sheet]]
+[[Category: Pang M]]
-[[Category: Dimer]]
-[[Category: Extracellular matrix]]
-[[Category: Galectin]]
-[[Category: Lectin]]
-[[Category: Secreted]]
-[[Category: Sugar binding protein]]

2km2

From Proteopedia

Current revision

Galectin-1 dimer

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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