7zor - Revision history

OCA at 08:05, 7 February 2024

2024-02-07T08:05:31Z

←Older revision		Revision as of 08:05, 7 February 2024
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	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zor OCA], [https://pdbe.org/7zor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zor RCSB], [https://www.ebi.ac.uk/pdbsum/7zor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zor ProSAT]</span></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=7zor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zor OCA], [https://pdbe.org/7zor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zor RCSB], [https://www.ebi.ac.uk/pdbsum/7zor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zor ProSAT]</span></td></tr>
	</table>		</table>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Sialic acid-binding Ig-like lectin 15 (Siglec-15) is an immune modulator and emerging cancer immunotherapy target. However, limited understanding of its structure and mechanism of action restrains the development of drug candidates that unleash its full therapeutic potential. In this study, we elucidate the crystal structure of Siglec-15 and its binding epitope via co-crystallization with an anti-Siglec-15 blocking antibody. Using saturation transfer-difference nuclear magnetic resonance (STD-NMR) spectroscopy and molecular dynamics simulations, we reveal Siglec-15 binding mode to alpha(2,3)- and alpha(2,6)-linked sialic acids and the cancer-associated sialyl-Tn (STn) glycoform. We demonstrate that binding of Siglec-15 to T cells, which lack STn expression, depends on the presence of alpha(2,3)- and alpha(2,6)-linked sialoglycans. Furthermore, we identify the leukocyte integrin CD11b as a Siglec-15 binding partner on human T cells. Collectively, our findings provide an integrated understanding of the structural features of Siglec-15 and emphasize glycosylation as a crucial factor in controlling T cell responses.
-
-	Structural insights into Siglec-15 reveal glycosylation dependency for its interaction with T cells through integrin CD11b.,Lenza MP, Egia-Mendikute L, Antonana-Vildosola A, Soares CO, Coelho H, Corzana F, Bosch A, Manisha P, Quintana JI, Oyenarte I, Unione L, Moure MJ, Azkargorta M, Atxabal U, Sobczak K, Elortza F, Sutherland JD, Barrio R, Marcelo F, Jimenez-Barbero J, Palazon A, Ereno-Orbea J Nat Commun. 2023 Jun 13;14(1):3496. doi: 10.1038/s41467-023-39119-8. PMID:37311743<ref>PMID:37311743</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 7zor" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 21:14, 28 June 2023

2023-06-28T21:14:25Z

←Older revision		Revision as of 21:14, 28 June 2023
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-	'''Unreleased structure'''

-	~~The entry~~ 7zor is ~~ON HOLD until Paper~~ Publication	+	==Structural insights of Siglec-15 reveal dependency in glycosylation for interaction with T cells through integrin CD11b==
		+	<StructureSection load='7zor' size='340' side='right'caption='[[7zor]], [[Resolution\|resolution]] 3.93Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[7zor]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZOR 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]] 3.933Å</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=7zor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zor OCA], [https://pdbe.org/7zor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zor RCSB], [https://www.ebi.ac.uk/pdbsum/7zor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zor ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Sialic acid-binding Ig-like lectin 15 (Siglec-15) is an immune modulator and emerging cancer immunotherapy target. However, limited understanding of its structure and mechanism of action restrains the development of drug candidates that unleash its full therapeutic potential. In this study, we elucidate the crystal structure of Siglec-15 and its binding epitope via co-crystallization with an anti-Siglec-15 blocking antibody. Using saturation transfer-difference nuclear magnetic resonance (STD-NMR) spectroscopy and molecular dynamics simulations, we reveal Siglec-15 binding mode to alpha(2,3)- and alpha(2,6)-linked sialic acids and the cancer-associated sialyl-Tn (STn) glycoform. We demonstrate that binding of Siglec-15 to T cells, which lack STn expression, depends on the presence of alpha(2,3)- and alpha(2,6)-linked sialoglycans. Furthermore, we identify the leukocyte integrin CD11b as a Siglec-15 binding partner on human T cells. Collectively, our findings provide an integrated understanding of the structural features of Siglec-15 and emphasize glycosylation as a crucial factor in controlling T cell responses.

-	~~Authors~~:	+	Structural insights into Siglec-15 reveal glycosylation dependency for its interaction with T cells through integrin CD11b.,Lenza MP, Egia-Mendikute L, Antonana-Vildosola A, Soares CO, Coelho H, Corzana F, Bosch A, Manisha P, Quintana JI, Oyenarte I, Unione L, Moure MJ, Azkargorta M, Atxabal U, Sobczak K, Elortza F, Sutherland JD, Barrio R, Marcelo F, Jimenez-Barbero J, Palazon A, Ereno-Orbea J Nat Commun. 2023 Jun 13;14(1):3496. doi: 10.1038/s41467-023-39119-8. PMID:37311743<ref>PMID:37311743</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 7zor" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Ereno-Orbea J]]
		+	[[Category: Jimenez-Barbero J]]
		+	[[Category: Lenza MP]]
		+	[[Category: Oyenarte I]]

OCA at 04:11, 8 June 2022

2022-06-08T04:11:25Z

←Older revision		Revision as of 04:11, 8 June 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7zor is ON HOLD	+	The entry 7zor is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7zor" [edit=sysop:move=sysop]

2022-05-04T11:48:50Z

Protected "7zor" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:48, 4 May 2022

OCA: New page: '''Unreleased structure''' The entry 7zor is ON HOLD Authors: Description: Category: Unreleased Structures

2022-05-04T11:48:49Z

New page: '''Unreleased structure''' The entry 7zor is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7zor is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]