View source for 5nlz


==GRIFIN (Crystallisation pH: 4.2)==
<StructureSection load='5nlz' size='340' side='right'caption='[[5nlz]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NLZ 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]] 1.149&#8491;</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=5nlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nlz OCA], [https://pdbe.org/5nlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nlz RCSB], [https://www.ebi.ac.uk/pdbsum/5nlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nlz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F1NZ18_CHICK F1NZ18_CHICK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Despite its natural abundance in lenses of vertebrates the physiological function(s) of the galectin-related inter-fiber protein (GRIFIN) is (are) still unclear. The same holds true for the significance of the unique interspecies (fish/birds vs mammals) variability in the capacity to bind lactose. In solution, ultracentrifugation and small angle X-ray scattering (at concentrations up to 9mg/mL) characterize the protein as compact and stable homodimer without evidence for aggregation. The crystal structure of chicken (C-)GRIFIN at seven pH values from 4.2 to 8.5 is reported, revealing compelling stability. Binding of lactose despite the Arg71Val deviation from the sequence signature of galectins matched the otherwise canonical contact pattern with thermodynamics of an enthalpically driven process. Upon lactose accommodation, the side chain of Arg50 is shifted for hydrogen bonding to the 3-hydroxyl of glucose. No evidence for a further ligand-dependent structural alteration was obtained in solution by measuring hydrogen/deuterium exchange mass spectrometrically in peptic fingerprints. The introduction of the Asn48Lys mutation, characteristic for mammalian GRIFINs that have lost lectin activity, lets labeled C-GRIFIN maintain capacity to stain tissue sections. Binding is no longer inhibitable by lactose, as seen for the wild-type protein. These results establish the basis for detailed structure-activity considerations and are a step to complete the structural description of all seven members of the galectin network in chicken.

Chicken GRIFIN: Structural characterization in crystals and in solution.,Ruiz FM, Gilles U, Ludwig AK, Sehad C, Shiao TC, Garcia Caballero G, Kaltner H, Lindner I, Roy R, Reusch D, Romero A, Gabius HJ Biochimie. 2018 Mar;146:127-138. doi: 10.1016/j.biochi.2017.12.003. Epub 2017 Dec, 15. PMID:29248541<ref>PMID:29248541</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nlz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Romero A]]
[[Category: Ruiz FM]]