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4bme

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Revision as of 08:54, 5 August 2016

Crystal structure of the N terminal domain of human Galectin 8, F19Y mutant

Structural highlights

4bme is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4bmb
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LEG8_HUMAN] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.^[1]

Publication Abstract from PubMed

Natural amino acid substitution by single-site nucleotide polymorphism can become a valuable tool for structure-activity correlations, especially if evidence for association to disease parameters exists. Focusing on the F19Y change in human galectin-8, connected clinically to rheumatoid arthritis, we here initiate the study of consequences of a single-site substitution in the carbohydrate recognition domain of this family of cellular effectors. We apply a strategically combined set of structural and cell biological techniques for comparing properties of the wild-type and variant proteins. The overall hydrodynamic behavior of the full-length protein and of the separate N-domain is not noticeably altered, but displacements in the F0 beta-strand of the beta-sandwich fold in the N-domain are induced, as evidenced by protein crystallography. Analysis of thermal stability by circular dichroism spectroscopy revealed perceptible differences for the full-length proteins, pointing to an impact of the substitution beyond the N-domain. In addition, small differences in thermodynamic parameters of carbohydrate binding are detected. On the level of two types of tumor cells, characteristics of binding appeared rather similar. In further comparison of the influence on proliferation, the variant proved to be more active as growth regulator in the six tested lines of neuroblastoma, erythroleukemia and colon adenocarcinoma. The seemingly subtle structural change identified here thus has functional implications in vitro, encouraging further analysis in autoimmune regulation and, in a broad context, in work with other natural single-site variants, using the documented combined strategy. DATABASE: The atomic coordinates and structure factors (codes 4BMB, 4BME) have been deposited in the Protein Data Bank.

Natural single amino acid polymorphism (F19Y) in human galectin-8: detection of structural alterations and increased growth-regulatory activity on tumor cells.,Ruiz FM, Scholz BA, Buzamet E, Kopitz J, Andre S, Menendez M, Romero A, Solis D, Gabius HJ FEBS J. 2014 Mar;281(5):1446-64. doi: 10.1111/febs.12716. Epub 2014 Feb 3. PMID:24418318^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ideo H, Matsuzaka T, Nonaka T, Seko A, Yamashita K. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. J Biol Chem. 2011 Apr 1;286(13):11346-55. Epub 2011 Feb 2. PMID:21288902 doi:10.1074/jbc.M110.195925
↑ Ruiz FM, Scholz BA, Buzamet E, Kopitz J, Andre S, Menendez M, Romero A, Solis D, Gabius HJ. Natural single amino acid polymorphism (F19Y) in human galectin-8: detection of structural alterations and increased growth-regulatory activity on tumor cells. FEBS J. 2014 Mar;281(5):1446-64. doi: 10.1111/febs.12716. Epub 2014 Feb 3. PMID:24418318 doi:http://dx.doi.org/10.1111/febs.12716

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bme"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the N terminal domain of human Galectin 8, F19Y mutant==
 <StructureSection load='4bme' size='340' side='right' caption='[[4bme]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LBT:ALPHA-LACTOSE'>LBT</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bmb|4bmb]]</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=4bme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bme OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bme RCSB], [http://www.ebi.ac.uk/pdbsum/4bme PDBsum]</span></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=4bme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bme OCA], [http://pdbe.org/4bme PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bme RCSB], [http://www.ebi.ac.uk/pdbsum/4bme PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bme ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4bme" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Galectin|Galectin]]
 == References ==
 <references/>

4bme

From Proteopedia

Revision as of 08:54, 5 August 2016

Crystal structure of the N terminal domain of human Galectin 8, F19Y mutant

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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