View source for 1qmo


==Structure of FRIL, a legume lectin that delays hematopoietic progenitor maturation==
<StructureSection load='1qmo' size='340' side='right'caption='[[1qmo]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qmo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Lablab_purpureus Lablab purpureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QMO 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]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1qmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmo OCA], [https://pdbe.org/1qmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qmo RCSB], [https://www.ebi.ac.uk/pdbsum/1qmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qmo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FRIL_LABPU FRIL_LABPU] Mannose-binding lectin (PubMed:9892687). Accommodates most effectively a non-reducing terminal alpha-d-mannosyl unit. Strongly precipitates murine IgM but not IgG (PubMed:9949194).<ref>PMID:9892687</ref> <ref>PMID:9949194</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/qm/1qmo_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=1qmo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Binding of multivalent glycoconjugates by lectins often leads to the formation of cross-linked complexes. Type I cross-links, which are one-dimensional, are formed by a divalent lectin and a divalent glycoconjugate. Type II cross-links, which are two or three-dimensional, occur when a lectin or glycoconjugate has a valence greater than two. Type II complexes are a source of additional specificity, since homogeneous type II complexes are formed in the presence of mixtures of lectins and glycoconjugates. This additional specificity is thought to become important when a lectin interacts with clusters of glycoconjugates, e.g. as is present on the cell surface. The cryst1al structure of the Glc/Man binding legume lectin FRIL in complex with a trisaccharide provides a molecular snapshot of how weak protein-protein interactions, which are not observed in solution, can become important when a cross-linked complex is formed. In solution, FRIL is a divalent dimer, but in the crystal FRIL forms a tetramer, which allows for the formation of an intricate type II cross-linked complex with the divalent trisaccharide. The dependence on weak protein-protein interactions can ensure that a specific type II cross-linked complex and its associated specificity can occur only under stringent conditions, which explains why lectins are often found forming higher-order oligomers.

The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL.,Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L J Mol Biol. 2000 Jun 16;299(4):875-83. PMID:10843844<ref>PMID:10843844</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qmo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Mannose-binding protein|Mannose-binding protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lablab purpureus]]
[[Category: Large Structures]]
[[Category: Chrispeels M]]
[[Category: Hamelryck TW]]
[[Category: Loris R]]
[[Category: Moore JG]]
[[Category: Wyns L]]