8a1f - Revision history

OCA at 14:19, 6 November 2024

2024-11-06T14:19:17Z

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 == Function ==
 [https://www.uniprot.org/uniprot/PTPRK_HUMAN PTPRK_HUMAN] Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.<ref>PMID:19836242</ref>
 == References ==
 <references/>

OCA at 08:08, 7 February 2024

2024-02-07T08:08:10Z

← Older revision		Revision as of 08:08, 7 February 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8a1f]] is a 2 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=8A1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1F FirstGlance]. <br>		<table><tr><td colspan='2'>[[8a1f]] is a 2 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=8A1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1F FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8a1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1f OCA], [https://pdbe.org/8a1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1f RCSB], [https://www.ebi.ac.uk/pdbsum/8a1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1f 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=8a1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1f OCA], [https://pdbe.org/8a1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1f RCSB], [https://www.ebi.ac.uk/pdbsum/8a1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/PTPRK_HUMAN PTPRK_HUMAN] Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.<ref>PMID:19836242</ref>		[https://www.uniprot.org/uniprot/PTPRK_HUMAN PTPRK_HUMAN] Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.<ref>PMID:19836242</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Type IIB receptor protein tyrosine phosphatases are cell surface transmembrane proteins that engage in cell adhesion via their extracellular domains (ECDs) and cell signaling via their cytoplasmic phosphatase domains. The ECDs of type IIB receptor protein tyrosine phosphatases form stable, homophilic, and trans interactions between adjacent cell membranes. Previous work has demonstrated how one family member, PTPRM, forms head-to-tail homodimers. However, as the interface was composed of residues conserved across the family, the determinants of homophilic specificity remain unknown. Here, we have solved the X-ray crystal structure of the membrane-distal N-terminal domains of PTPRK that form a head-to-tail dimer consistent with intermembrane adhesion. Comparison with the PTPRM structure demonstrates interdomain conformational differences that may define homophilic specificity. Using small-angle X-ray scattering, we determined the solution structures of the full-length ECDs of PTPRM and PTPRK, identifying that both are rigid extended molecules that differ in their overall long-range conformation. Furthermore, we identified one residue, W351, within the interaction interface that differs between PTPRM and PTPRK and showed that mutation to glycine, the equivalent residue in PTPRM, abolishes PTPRK dimer formation in vitro. This comparison of two members of the receptor tyrosine phosphatase family suggests that homophilic specificity is driven by a combination of shape complementarity and specific but limited sequence differences.

	Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains.,Hay IM, Shamin M, Caroe ER, Mohammed ASA, Svergun DI, Jeffries CM, Graham SC, Sharpe HJ, Deane JE J Biol Chem. 2023 Jan;299(1):102750. doi: 10.1016/j.jbc.2022.102750. Epub 2022 , Nov 25. PMID:36436563<ref>PMID:36436563</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 8a1f" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:51, 15 March 2023

2023-03-15T09:51:06Z

← Older revision		Revision as of 09:51, 15 March 2023
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	~~'''Unreleased structure'''~~

	~~The entry~~ 8a1f is ~~ON HOLD until Paper~~ Publication		==Human PTPRK N-terminal domains MAM-Ig-FN1==
			<StructureSection load='8a1f' size='340' side='right'caption='[[8a1f]], [[Resolution\|resolution]] 3.00Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[8a1f]] is a 2 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=8A1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1F FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=8a1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1f OCA], [https://pdbe.org/8a1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1f RCSB], [https://www.ebi.ac.uk/pdbsum/8a1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1f ProSAT]</span></td></tr>
			</table>
			== Function ==
			[https://www.uniprot.org/uniprot/PTPRK_HUMAN PTPRK_HUMAN] Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.<ref>PMID:19836242</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Type IIB receptor protein tyrosine phosphatases are cell surface transmembrane proteins that engage in cell adhesion via their extracellular domains (ECDs) and cell signaling via their cytoplasmic phosphatase domains. The ECDs of type IIB receptor protein tyrosine phosphatases form stable, homophilic, and trans interactions between adjacent cell membranes. Previous work has demonstrated how one family member, PTPRM, forms head-to-tail homodimers. However, as the interface was composed of residues conserved across the family, the determinants of homophilic specificity remain unknown. Here, we have solved the X-ray crystal structure of the membrane-distal N-terminal domains of PTPRK that form a head-to-tail dimer consistent with intermembrane adhesion. Comparison with the PTPRM structure demonstrates interdomain conformational differences that may define homophilic specificity. Using small-angle X-ray scattering, we determined the solution structures of the full-length ECDs of PTPRM and PTPRK, identifying that both are rigid extended molecules that differ in their overall long-range conformation. Furthermore, we identified one residue, W351, within the interaction interface that differs between PTPRM and PTPRK and showed that mutation to glycine, the equivalent residue in PTPRM, abolishes PTPRK dimer formation in vitro. This comparison of two members of the receptor tyrosine phosphatase family suggests that homophilic specificity is driven by a combination of shape complementarity and specific but limited sequence differences.

	~~Authors~~: Hay, I.M., Graham, S.C.~~, Sharpe, H~~.J., ~~Deane, J.E~~.		Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains.,Hay IM, Shamin M, Caroe ER, Mohammed ASA, Svergun DI, Jeffries CM, Graham SC, Sharpe HJ, Deane JE J Biol Chem. 2023 Jan;299(1):102750. doi: 10.1016/j.jbc.2022.102750. Epub 2022 , Nov 25. PMID:36436563<ref>PMID:36436563</ref>

	~~Description: Human PTPRK N~~-~~terminal domains MAM~~-~~Ig-FN1~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased~~ Structures]]		</div>
	[[Category: ~~Sharpe, H.J~~]]		<div class="pdbe-citations 8a1f" style="background-color:#fffaf0;"></div>
	[[Category: ~~Hay, I.M~~]]		== References ==
	[[Category: ~~Deane, J.E~~]]		<references/>
	[[Category: ~~Graham, S.C~~]]		__TOC__
			</StructureSection>
			[[Category: Homo sapiens]]
			[[Category: Large Structures]]
			[[Category: Deane JE]]
			[[Category: Graham SC]]
			[[Category: Hay IM]]
			[[Category: Sharpe HJ]]

OCA at 07:16, 22 June 2022

2022-06-22T07:16:25Z

← Older revision		Revision as of 07:16, 22 June 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8a1f is ON HOLD		The entry 8a1f is ON HOLD until Paper Publication

	Authors: Hay, I.M., Graham, S.C., Sharpe, H.J., Deane, J.E.		Authors: Hay, I.M., Graham, S.C., Sharpe, H.J., Deane, J.E.

	Description: PTPRK ~~MIFN1~~ domains		Description: Human PTPRK N-terminal domains MAM-Ig-FN1
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Sharpe, H.J]]		[[Category: Sharpe, H.J]]
	[[Category: Hay, I.M]]		[[Category: Hay, I.M]]
			[[Category: Deane, J.E]]
	[[Category: Graham, S.C]]		[[Category: Graham, S.C]]
	~~[[Category: Deane, J.E]]~~

OCA: Protected "8a1f" [edit=sysop:move=sysop]

2022-06-08T04:23:04Z

Protected "8a1f" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:23, 8 June 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8a1f is ON HOLD Authors: Hay, I.M., Graham, S.C., Sharpe, H.J., Deane, J.E. Description: PTPRK MIFN1 domains Category: Unreleased Structures [[...

2022-06-08T04:23:03Z

New page: '''Unreleased structure''' The entry 8a1f is ON HOLD Authors: Hay, I.M., Graham, S.C., Sharpe, H.J., Deane, J.E. Description: PTPRK MIFN1 domains Category: Unreleased Structures [[...

New page

'''Unreleased structure'''

The entry 8a1f is ON HOLD

Authors: Hay, I.M., Graham, S.C., Sharpe, H.J., Deane, J.E.

Description: PTPRK MIFN1 domains
[[Category: Unreleased Structures]]
[[Category: Sharpe, H.J]]
[[Category: Hay, I.M]]
[[Category: Graham, S.C]]
[[Category: Deane, J.E]]