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[[Image:1slt.jpg|left|200px]]
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{{STRUCTURE_1slt|  PDB=1slt  |  SCENE=  }}
'''STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN'''


==STRUCTURE OF S-LECTIN, A DEVELOPMENTALLY REGULATED VERTEBRATE BETA-GALACTOSIDE BINDING PROTEIN==
<StructureSection load='1slt' size='340' side='right'caption='[[1slt]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1slt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SLT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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=1slt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1slt OCA], [https://pdbe.org/1slt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1slt RCSB], [https://www.ebi.ac.uk/pdbsum/1slt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1slt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LEG1_BOVIN LEG1_BOVIN] May regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity (By similarity).
== 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/sl/1slt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1slt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers associate to form an extended beta-sandwich, each with the same jelly roll topology typical of legume lectins but with dramatically trimmed loops and with different dimer association. Each monomer binds one N-acetyllactosamine molecule in a topologically and spatially different site than that of legume lectins. The carbohydrate-binding site provides an unprecedented paradigm for carbohydrate binding, with a unique network of salt bridges. The specificity for beta-galactose arises from intricate interactions that constrain the position of the O4 atom.


==Overview==
Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.,Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1428-32. PMID:8108426<ref>PMID:8108426</ref>
The crystal structure of a 14-kDa bovine spleen S-lectin complexed with the disaccharide N-acetyllactosamine at 1.9-A resolution reveals a surprising structural relationship to legume lectins, despite the lack of sequence homology. Two monomers associate to form an extended beta-sandwich, each with the same jelly roll topology typical of legume lectins but with dramatically trimmed loops and with different dimer association. Each monomer binds one N-acetyllactosamine molecule in a topologically and spatially different site than that of legume lectins. The carbohydrate-binding site provides an unprecedented paradigm for carbohydrate binding, with a unique network of salt bridges. The specificity for beta-galactose arises from intricate interactions that constrain the position of the O4 atom.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1SLT is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLT OCA].
</div>
<div class="pdbe-citations 1slt" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein., Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O, Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1428-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8108426 8108426]
*[[Galectin 3D structures|Galectin 3D structures]]
[[Category: Single protein]]
== References ==
[[Category: Herzberg, O.]]
<references/>
[[Category: Liao, D I.]]
__TOC__
[[Category: Lectin]]
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:51:46 2008''
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Herzberg O]]
[[Category: Liao D-I]]
Retrieved from "https://proteopedia.org/1slt"