Latrophilin - Revision history

Michal Harel at 05:38, 18 June 2023

Michal Harel — Sun, 18 Jun 2023 05:38:53 GMT

←Older revision		Revision as of 05:38, 18 June 2023
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	**[[5afb]] – hLAT-3 olfactomedin and lectin domains 97-495<br />		**[[5afb]] – hLAT-3 olfactomedin and lectin domains 97-495<br />
	**[[5cmn]] – hLAT-3 olfactomedin domain + FLRT3<br />		**[[5cmn]] – hLAT-3 olfactomedin domain + FLRT3<br />
		+	**[[8djg]] – hLAT-3 residues 24-126 + antibody<br />
		+	**[[7wy5]], [[7wy8]], [[7wyb]] – hLAT-3 + nanobody + GS – Cryo EM<br />
		+	**[[7sf7]] – hLAT-3 residues 842-1138 + GS – Cryo EM<br />
		+	**[[7x10]] – hLAT-3 + Scfv + GS – Cryo EM<br />
	**[[4yeb]] – mLAT-3 + FLRT3 <br />		**[[4yeb]] – mLAT-3 + FLRT3 <br />
	**[[6jbu]] – mLAT-3 olfactomedin domain + FLRT3<br />		**[[6jbu]] – mLAT-3 olfactomedin domain + FLRT3<br />

Michal Harel — Mon, 31 Aug 2020 09:04:57 GMT

←Older revision		Revision as of 09:04, 31 August 2020
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	**[[5ftt]], [[5ftu]] – hLAT-3 + FLRT2 + netrin receptor - human<br />		**[[5ftt]], [[5ftu]] – hLAT-3 + FLRT2 + netrin receptor - human<br />
		+	**[[4rmk]], [[4rml]] – hLAT-3 olfactomedin domain 199-495<br />
		+	**[[5afb]] – hLAT-3 olfactomedin and lectin domains 97-495<br />
	**[[5cmn]] – hLAT-3 olfactomedin domain + FLRT3<br />		**[[5cmn]] – hLAT-3 olfactomedin domain + FLRT3<br />
	**[[4yeb]] – mLAT-3 + FLRT3 <br />		**[[4yeb]] – mLAT-3 + FLRT3 <br />
-	**[[~~4rmk]], [[4rml~~]] – ~~hLAT~~-3 olfactomedin domain<br />	+	**[[6jbu]] – mLAT-3 olfactomedin domain + FLRT3<br />
-	**[[~~5afb~~]] – ~~hLAT~~-3 olfactomedin ~~and lectin domains~~<br />	+	**[[6ska]], [[6ske]], [[6vhh]] – mLAT-3 olfactomedin domain + teneurin-2<br />
	}}		}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel — Mon, 31 Aug 2020 08:50:13 GMT

←Older revision		Revision as of 08:50, 31 August 2020
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	</StructureSection>		</StructureSection>
-	==3D structures of ~~latropilin~~==	+	==3D structures of latrophilin==

	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}		Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

Michal Harel — Mon, 31 Aug 2020 08:49:12 GMT

←Older revision		Revision as of 08:49, 31 August 2020
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	</StructureSection>		</StructureSection>
-	==3D structures of ~~lactophilin~~==	+	==3D structures of latropilin==

	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}		Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

Alexander Berchansky — Thu, 04 Jul 2019 10:46:38 GMT

←Older revision		Revision as of 10:46, 4 July 2019
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	== Structural highlights ==		== Structural highlights ==
-	The high-affinity of the LAT-3/FLRT3 complex is achieved by a combination of interactions between the <scene name='74/748875/Cv/2'>round face of LAT-3 and the concave surface of FLRT3</scene><ref>PMID:26235030</ref>. <scene name='74/748875/Cv/3'>All interactions</scene>.	+	The high-affinity of the LAT-3/FLRT3 complex is achieved by a combination of interactions between the <scene name='74/748875/Cv/4'>round face of LAT-3 and the concave surface of FLRT3</scene><ref>PMID:26235030</ref>. <scene name='74/748875/Cv/5'>All interactions</scene>.

	</StructureSection>		</StructureSection>

Joel L. Sussman — Fri, 20 Oct 2017 16:14:49 GMT

←Older revision		Revision as of 16:14, 20 October 2017
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-	<StructureSection load='~~5cmn~~' size='400' side='right' caption='Human latrophilin-3 olfactomedin domain (magenta) complex with leucine-rich repeat transmembrane protein 3 (blue) and Ca+2 ion (green) (PDB code [[5cmn]]) ' scene='74/748875/Cv/1'>	+	<StructureSection load='' size='400' side='right' caption='Human latrophilin-3 olfactomedin domain (magenta) complex with leucine-rich repeat transmembrane protein 3 (blue) and Ca+2 ion (green) (PDB code [[5cmn]]) ' scene='74/748875/Cv/1'>

Michal Harel — Fri, 20 Oct 2017 13:31:38 GMT

←Older revision		Revision as of 13:31, 20 October 2017
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-	<StructureSection load='5cmn' size='400' side='right' caption='Human latrophilin-3 olfactomedin domain (magenta) complex with leucine-rich repeat transmembrane protein 3 (~~deep skyblue~~) and Ca+2 ion (green) (PDB code [[5cmn]]) ' scene='74/748875/Cv/1'>	+	<StructureSection load='5cmn' size='400' side='right' caption='Human latrophilin-3 olfactomedin domain (magenta) complex with leucine-rich repeat transmembrane protein 3 (blue) and Ca+2 ion (green) (PDB code [[5cmn]]) ' scene='74/748875/Cv/1'>


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	== References ==		== References ==
	<references/>		<references/>
		+	[[Category:Topic Page]]

Michal Harel — Sun, 02 Jul 2017 10:12:40 GMT

←Older revision		Revision as of 10:12, 2 July 2017
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-	<StructureSection load='5cmn' size='~~450~~' side='right' caption='Human latrophilin-3 olfactomedin domain (magenta) complex with leucine-rich repeat transmembrane protein 3 (~~deepskyblue~~) and Ca+2 ion (green) (PDB code [[5cmn]]) ' scene='74/748875/Cv/1'>	+	<StructureSection load='5cmn' size='400' side='right' caption='Human latrophilin-3 olfactomedin domain (magenta) complex with leucine-rich repeat transmembrane protein 3 (deep skyblue) and Ca+2 ion (green) (PDB code [[5cmn]]) ' scene='74/748875/Cv/1'>

Alexander Berchansky — Wed, 21 Dec 2016 15:01:37 GMT

←Older revision		Revision as of 15:01, 21 December 2016
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	== Structural highlights ==		== Structural highlights ==
-	The high-affinity of the LAT-3/FLRT3 complex is achieved by a combination of interactions between the <scene name='74/748875/Cv/2'>round face of LAT-3 and the concave surface of FLRT3</scene><ref>PMID:26235030</ref>.	+	The high-affinity of the LAT-3/FLRT3 complex is achieved by a combination of interactions between the <scene name='74/748875/Cv/2'>round face of LAT-3 and the concave surface of FLRT3</scene><ref>PMID:26235030</ref>. <scene name='74/748875/Cv/3'>All interactions</scene>.

	</StructureSection>		</StructureSection>

Alexander Berchansky — Wed, 21 Dec 2016 14:49:15 GMT

←Older revision		Revision as of 14:49, 21 December 2016
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	== Structural highlights ==		== Structural highlights ==
-	The high-affinity of the LAT-3/FLRT3 complex is achieved by a combination of interactions between the round face of LAT-3 and the concave surface of FLRT3<ref>PMID:26235030</ref>.	+	The high-affinity of the LAT-3/FLRT3 complex is achieved by a combination of interactions between the <scene name='74/748875/Cv/2'>round face of LAT-3 and the concave surface of FLRT3</scene><ref>PMID:26235030</ref>.

	</StructureSection>		</StructureSection>