4c4p - Revision history

OCA at 11:08, 9 May 2024

OCA — Thu, 09 May 2024 11:08:48 GMT

←Older revision		Revision as of 11:08, 9 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c4p]] 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=4C4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c4p]] 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=4C4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [https://pdbe.org/4c4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [https://www.ebi.ac.uk/pdbsum/4c4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4p 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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [https://pdbe.org/4c4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [https://www.ebi.ac.uk/pdbsum/4c4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN]] The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.<ref>PMID:15601896</ref> <ref>PMID:15689490</ref> <ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:20890297</ref> <ref>PMID:21282656</ref>	+	[https://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN] The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.<ref>PMID:15601896</ref> <ref>PMID:15689490</ref> <ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:20890297</ref> <ref>PMID:21282656</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Rab small GTPases are the master regulators of intracellular trafficking in eukaryotes. They mediate spatial and temporal recruitment of effector proteins to distinct cellular compartments through GTP-induced changes in their conformation. Despite numerous structural studies, the molecular basis for Rab/effector specificity and subsequent biological activity remains poorly understood. Rab25, also known as Rab11c, which is epithelial-specific, has been heavily implicated in ovarian cancer development and independently appears to act as a tumour suppressor in the context of a distinct subset of carcinomas. Here, we show that Rab25 associates with FIP2 and can recruit this effector protein to endosomal membranes. We report the crystal structure of Rab25 in complex with the C-terminal region of FIP2, which consists of a central dimeric FIP2 coiled-coil that mediates a heterotetrameric Rab25-(FIP2)2-Rab25 complex. Thermodynamic analyses show that, despite a relatively conserved interface, FIP2 binds to Rab25 with an approximate 3-fold weaker affinity than to Rab11a. Reduced affinity is mainly associated with lower enthalpic gains for Rab25:FIP2 complex formation, and can be attributed to subtle differences in the conformations of switch 1 and switch 2. These cellular, structural and thermodynamic studies provide insight into the Rab11/Rab25 subfamily of small GTPases that regulate endosomal trafficking pathways in eukaryotes.
		+
		+	Structural and functional analysis of FIP2 binding to the endosome-localised Rab25 GTPase.,Lall P, Horgan CP, Oda S, Franklin E, Sultana A, Hanscom SR, McCaffrey MW, Khan AR Biochim Biophys Acta. 2013 Sep 19. pii: S1570-9639(13)00317-8. doi:, 10.1016/j.bbapap.2013.09.005. PMID:24056041<ref>PMID:24056041</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c4p" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:26, 7 September 2022

OCA — Wed, 07 Sep 2022 17:26:53 GMT

←Older revision		Revision as of 17:26, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c4p' size='340' side='right'caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4c4p' size='340' side='right'caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C4P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c4p]] 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=4C4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [~~http~~://pdbe.org/4c4p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c4p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4p 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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [https://pdbe.org/4c4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [https://www.ebi.ac.uk/pdbsum/4c4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN]] The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.<ref>PMID:15601896</ref> <ref>PMID:15689490</ref> <ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:20890297</ref> <ref>PMID:21282656</ref> [[http://www.uniprot.org/uniprot/RFIP2_HUMAN RFIP2_HUMAN]] A Rab11 effector protein acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Binds preferentially to phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA). Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity.<ref>PMID:12364336</ref> <ref>PMID:15304524</ref> <ref>PMID:16775013</ref> <ref>PMID:19542231</ref>	+	[[https://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN]] The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.<ref>PMID:15601896</ref> <ref>PMID:15689490</ref> <ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:20890297</ref> <ref>PMID:21282656</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Rab small GTPases are the master regulators of intracellular trafficking in eukaryotes. They mediate spatial and temporal recruitment of effector proteins to distinct cellular compartments through GTP-induced changes in their conformation. Despite numerous structural studies, the molecular basis for Rab/effector specificity and subsequent biological activity remains poorly understood. Rab25, also known as Rab11c, which is epithelial-specific, has been heavily implicated in ovarian cancer development and independently appears to act as a tumour suppressor in the context of a distinct subset of carcinomas. Here, we show that Rab25 associates with FIP2 and can recruit this effector protein to endosomal membranes. We report the crystal structure of Rab25 in complex with the C-terminal region of FIP2, which consists of a central dimeric FIP2 coiled-coil that mediates a heterotetrameric Rab25-(FIP2)2-Rab25 complex. Thermodynamic analyses show that, despite a relatively conserved interface, FIP2 binds to Rab25 with an approximate 3-fold weaker affinity than to Rab11a. Reduced affinity is mainly associated with lower enthalpic gains for Rab25:FIP2 complex formation, and can be attributed to subtle differences in the conformations of switch 1 and switch 2. These cellular, structural and thermodynamic studies provide insight into the Rab11/Rab25 subfamily of small GTPases that regulate endosomal trafficking pathways in eukaryotes.	+
-		+
-	Structural and functional analysis of FIP2 binding to the endosome-localised Rab25 GTPase.,Lall P, Horgan CP, Oda S, Franklin E, Sultana A, Hanscom SR, McCaffrey MW, Khan AR Biochim Biophys Acta. 2013 Sep 19. pii: S1570-9639(13)00317-8. doi:, 10.1016/j.bbapap.2013.09.005. PMID:24056041<ref>PMID:24056041</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c4p" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
-	*[[Ras-related protein Rab\|Ras-related protein Rab]]	+	*[[Ras-related protein Rab 3D structures\|Ras-related protein Rab 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Khan~~, A R~~]]	+	[[Category: Khan AR]]
-	[[Category: Sultana, A]]	+	[[Category: Sultana A]]
-	~~[[Category: Effector]]~~	+
-	~~[[Category: Endosome]]~~	+
-	~~[[Category: Protein transport]]~~	+
-	~~[[Category: Vesicle trafficking~~]]	+

OCA at 16:48, 28 August 2019

OCA — Wed, 28 Aug 2019 16:48:18 GMT

←Older revision		Revision as of 16:48, 28 August 2019
Line 1:		Line 1:

	==Crystal Structure of Wild-Type Rab11 Complexed to FIP2==		==Crystal Structure of Wild-Type Rab11 Complexed to FIP2==
-	<StructureSection load='4c4p' size='340' side='right' caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4c4p' size='340' side='right'caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4P FirstGlance]. <br>
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4c4p" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4c4p" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ras-related protein Rab\|Ras-related protein Rab]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Khan, A R]]		[[Category: Khan, A R]]
	[[Category: Sultana, A]]		[[Category: Sultana, A]]

OCA at 17:35, 16 November 2017

OCA — Thu, 16 Nov 2017 17:35:28 GMT

←Older revision		Revision as of 17:35, 16 November 2017
Line 1:		Line 1:
		+
	==Crystal Structure of Wild-Type Rab11 Complexed to FIP2==		==Crystal Structure of Wild-Type Rab11 Complexed to FIP2==
	<StructureSection load='4c4p' size='340' side='right' caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4c4p' size='340' side='right' caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4P FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [http://pdbe.org/4c4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [http://www.ebi.ac.uk/pdbsum/4c4p 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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [http://pdbe.org/4c4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [http://www.ebi.ac.uk/pdbsum/4c4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Khan, A R]]		[[Category: Khan, A R]]
	[[Category: Sultana, A]]		[[Category: Sultana, A]]

OCA at 07:47, 30 September 2015

OCA — Wed, 30 Sep 2015 07:47:22 GMT

←Older revision		Revision as of 07:47, 30 September 2015
Line 2:		Line 2:
	<StructureSection load='4c4p' size='340' side='right' caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4c4p' size='340' side='right' caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4P FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [http://www.ebi.ac.uk/pdbsum/4c4p 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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [http://pdbe.org/4c4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [http://www.ebi.ac.uk/pdbsum/4c4p PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4c4p" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Homo sapiens]]
	[[Category: Khan, A R]]		[[Category: Khan, A R]]
	[[Category: Sultana, A]]		[[Category: Sultana, A]]

OCA at 17:03, 24 December 2014

OCA — Wed, 24 Dec 2014 17:03:15 GMT

←Older revision		Revision as of 17:03, 24 December 2014
Line 6:		Line 6:
	<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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [http://www.ebi.ac.uk/pdbsum/4c4p 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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [http://www.ebi.ac.uk/pdbsum/4c4p PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN]] The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.<ref>PMID:15601896</ref> <ref>PMID:15689490</ref> <ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:20890297</ref> <ref>PMID:21282656</ref> [[http://www.uniprot.org/uniprot/RFIP2_HUMAN RFIP2_HUMAN]] A Rab11 effector protein acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Binds preferentially to phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA). Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity.<ref>PMID:12364336</ref> <ref>PMID:15304524</ref> <ref>PMID:16775013</ref> <ref>PMID:19542231</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:54, 21 December 2014

OCA — Sun, 21 Dec 2014 09:54:20 GMT

←Older revision		Revision as of 09:54, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4c4p\| PDB=4c4p \| SCENE= }}~~	+	==Crystal Structure of Wild-Type Rab11 Complexed to FIP2==
-	===Crystal Structure of Wild-Type Rab11 Complexed to FIP2===	+	<StructureSection load='4c4p' size='340' side='right' caption='[[4c4p]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24056041}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4c4p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4P FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4c4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4p RCSB], [http://www.ebi.ac.uk/pdbsum/4c4p PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Rab small GTPases are the master regulators of intracellular trafficking in eukaryotes. They mediate spatial and temporal recruitment of effector proteins to distinct cellular compartments through GTP-induced changes in their conformation. Despite numerous structural studies, the molecular basis for Rab/effector specificity and subsequent biological activity remains poorly understood. Rab25, also known as Rab11c, which is epithelial-specific, has been heavily implicated in ovarian cancer development and independently appears to act as a tumour suppressor in the context of a distinct subset of carcinomas. Here, we show that Rab25 associates with FIP2 and can recruit this effector protein to endosomal membranes. We report the crystal structure of Rab25 in complex with the C-terminal region of FIP2, which consists of a central dimeric FIP2 coiled-coil that mediates a heterotetrameric Rab25-(FIP2)2-Rab25 complex. Thermodynamic analyses show that, despite a relatively conserved interface, FIP2 binds to Rab25 with an approximate 3-fold weaker affinity than to Rab11a. Reduced affinity is mainly associated with lower enthalpic gains for Rab25:FIP2 complex formation, and can be attributed to subtle differences in the conformations of switch 1 and switch 2. These cellular, structural and thermodynamic studies provide insight into the Rab11/Rab25 subfamily of small GTPases that regulate endosomal trafficking pathways in eukaryotes.

-	~~==Function==~~	+	Structural and functional analysis of FIP2 binding to the endosome-localised Rab25 GTPase.,Lall P, Horgan CP, Oda S, Franklin E, Sultana A, Hanscom SR, McCaffrey MW, Khan AR Biochim Biophys Acta. 2013 Sep 19. pii: S1570-9639(13)00317-8. doi:, 10.1016/j.bbapap.2013.09.005. PMID:24056041<ref>PMID:24056041</ref>
-	~~[[http://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN]] The small GTPases Rab are key regulators~~ of ~~intracellular membrane trafficking, from~~ the ~~formation of transport vesicles to their fusion with membranes~~. ~~Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation~~, ~~movement~~, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, ~~RAB8A~~, ~~the exocyst complex~~, ~~PARD3~~, ~~PRKCI~~, ~~ANXA2~~, ~~CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis~~. ~~Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells~~. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (~~receptor of Fc region of monomeric Ig G~~) ~~to basolateral membranes~~. ~~May also play a role in melanosome transport and release from melanocytes.<ref>PMID~~:~~15601896</ref> <ref>PMID:15689490</ref> <ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:20890297</ref> <ref>PMID:21282656</ref> [[http://www~~.~~uniprot.org~~/~~uniprot/RFIP2_HUMAN RFIP2_HUMAN]] A Rab11 effector protein acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane~~. ~~Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles~~. ~~Binds preferentially to phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA)~~. ~~Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane~~. ~~Also acts as a regulator of cell polarity~~.~~<ref>~~PMID:~~12364336</ref> <ref>PMID:15304524</ref> <ref>PMID:16775013</ref>~~ <ref>PMID:~~19542231~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4c4p]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024056041</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Khan, A R.]]	+	[[Category: Khan, A R]]
-	[[Category: Sultana, A.]]	+	[[Category: Sultana, A]]
	[[Category: Effector]]		[[Category: Effector]]
	[[Category: Endosome]]		[[Category: Endosome]]
	[[Category: Protein transport]]		[[Category: Protein transport]]
	[[Category: Vesicle trafficking]]		[[Category: Vesicle trafficking]]

OCA at 05:52, 2 October 2013

OCA — Wed, 02 Oct 2013 05:52:52 GMT

←Older revision		Revision as of 05:52, 2 October 2013
Line 1:		Line 1:
	{{STRUCTURE_4c4p\| PDB=4c4p \| SCENE= }}		{{STRUCTURE_4c4p\| PDB=4c4p \| SCENE= }}
	===Crystal Structure of Wild-Type Rab11 Complexed to FIP2===		===Crystal Structure of Wild-Type Rab11 Complexed to FIP2===
		+	{{ABSTRACT_PUBMED_24056041}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024056041</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Khan, A R.]]		[[Category: Khan, A R.]]

OCA: Protected "4c4p" [edit=sysop:move=sysop]

OCA — Fri, 20 Sep 2013 04:18:42 GMT

Protected "4c4p" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:18, 20 September 2013

OCA: New page: {{STRUCTURE_4c4p| PDB=4c4p | SCENE= }} ===Crystal Structure of Wild-Type Rab11 Complexed to FIP2=== ==Function== http://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN The small ...

OCA — Fri, 20 Sep 2013 04:18:34 GMT

New page: {{STRUCTURE_4c4p| PDB=4c4p | SCENE= }} ===Crystal Structure of Wild-Type Rab11 Complexed to FIP2=== ==Function== http://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN The small ...

New page

{{STRUCTURE_4c4p| PDB=4c4p | SCENE= }}
===Crystal Structure of Wild-Type Rab11 Complexed to FIP2===

==Function==
[[http://www.uniprot.org/uniprot/RB11A_HUMAN RB11A_HUMAN]] The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.<ref>PMID:15601896</ref> <ref>PMID:15689490</ref> <ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:20890297</ref> <ref>PMID:21282656</ref> [[http://www.uniprot.org/uniprot/RFIP2_HUMAN RFIP2_HUMAN]] A Rab11 effector protein acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Binds preferentially to phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA). Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity.<ref>PMID:12364336</ref> <ref>PMID:15304524</ref> <ref>PMID:16775013</ref> <ref>PMID:19542231</ref>

==About this Structure==
[[4c4p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4P OCA].

==Reference==
<references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Khan, A R.]]
[[Category: Sultana, A.]]
[[Category: Effector]]
[[Category: Endosome]]
[[Category: Protein transport]]
[[Category: Vesicle trafficking]]