4hl0: Difference between revisions

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{{STRUCTURE_4hl0| PDB=4hl0 | SCENE= }}
==Crystal structure of full-length Toxascaris leonina galectin==
===Crystal structure of full-length Toxascaris leonina galectin===
<StructureSection load='4hl0' size='340' side='right' caption='[[4hl0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
{{ABSTRACT_PUBMED_23385453}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4hl0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxascaris_leonina Toxascaris leonina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HL0 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nv1|3nv1]]</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=4hl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hl0 RCSB], [http://www.ebi.ac.uk/pdbsum/4hl0 PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The full-length crystal structure of Toxascaris leonine galectin (Tl-gal), a galectin-9 homologue protein, was determined at a resolution of 2.0 A. Galectin-9 exhibits a variety of biological functions, including cell aggregation, eosinophil chemoattraction, activation and apoptosis of murine thymocytes, T cells and human melanoma cells. Similar to this galectin, Tl-gal may function as a regulatory molecule in the host immune system; however, no molecular or structural information has been reported for Tl-gal. Moreover, until now, there have been no reports of a full-length galectin structure. There are two molecules of Tl-gal per asymmetric unit in space group P2(1)2(1)2(1), and the N-terminal and C-terminal carbohydrate-recognition domains (NCRD and CCRD) of Tl-gal are composed of six-stranded beta-sheets and five-stranded beta-sheets with a short alpha-helix. The NCRD of Tl-gal resembles that of human galectin-7 and its CCRD resembles human galectin-9, but the residues in the interface and loop regions of the NCRD and CCRD are flexible and are related to interaction. Engagement of the T-cell immunoglobulin mucin-3 (Tim-3) immunoglobulin variable (IgV) domain by a galectin-9 ligand is known to be important for appropriate termination of T-helper 1 immune responses. To investigate the binding site of Tl-gal, the interaction between Tl-gal and Tim-3 was modelled. Tim-3 is docked into a major groove of the Tl-gal structure, which is larger and deeper than the minor groove. The structural information presented here will provide insight into the development of novel anti-inflammatory agents or selective modulators of immune response.


==About this Structure==
Structure of full-length Toxascaris leonina galectin with two carbohydrate-recognition domains.,Jeong MS, Hwang HG, Yu HS, Jang SB Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):168-75. doi:, 10.1107/S0907444912045106. Epub 2013 Jan 16. PMID:23385453<ref>PMID:23385453</ref>
[[4hl0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxascaris_leonina Toxascaris leonina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HL0 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:023385453</ref><references group="xtra"/><references/>
</div>
 
==See Also==
*[[Galectin|Galectin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Toxascaris leonina]]
[[Category: Toxascaris leonina]]
[[Category: Jeong, M S.]]
[[Category: Jeong, M S]]
[[Category: A regulatory molecule]]
[[Category: A regulatory molecule]]
[[Category: Carbohydrate recognition domain]]
[[Category: Carbohydrate recognition domain]]

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