5yzb - Revision history

OCA at 10:25, 27 March 2024

OCA — Wed, 27 Mar 2024 10:25:52 GMT

←Older revision		Revision as of 10:25, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='5yzb' size='340' side='right'caption='[[5yzb]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='5yzb' size='340' side='right'caption='[[5yzb]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5yzb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5YZB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5yzb]] is a 1 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=5YZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YZB FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5yzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzb OCA], [~~http~~://pdbe.org/5yzb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5yzb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5yzb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzb ProSAT]</span></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]] 2.8Å</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=5yzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzb OCA], [https://pdbe.org/5yzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yzb RCSB], [https://www.ebi.ac.uk/pdbsum/5yzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzb ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DPYL2_HUMAN DPYL2_HUMAN]] Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (By similarity). Plays a role in neuron projection morphogenesis.<ref>PMID:11477421</ref> <ref>PMID:15466863</ref>	+	[https://www.uniprot.org/uniprot/DPYL2_HUMAN DPYL2_HUMAN] Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (By similarity). Plays a role in neuron projection morphogenesis.<ref>PMID:11477421</ref> <ref>PMID:15466863</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Collapsin response mediator protein 2 (CRMP2) regulates neuronal polarity by controlling microtubule dynamics. CRMP2 activity is regulated by semaphorin-induced phosphorylation at the C-terminal tail domain. Unphosphorylated CRMP2 induces effective axonal microtubule formation to give the axonal characteristics to a neurite, whereas phosphorylated CRMP2 leads to the apparently opposite effect, growth cone collapse. We have recently characterized the structural detail of CRMP2-induced axonal microtubule formation (Niwa et al. (2017) Sci. Rep., 7: 10681). CRMP2 forms the hetero-trimer with GTP-tubulin to induce effective axonal microtubule formation in the future axon. Phosphorylation of CRMP2 has been reported to decrease the affinity between CRMP2 and the microtubule, albeit the molecular mechanisms of how the phosphorylation of CRMP2 changes the structure to achieve distinct effects from unphosphorylated CRMP2 is not well understood. Here we performed a series of biochemical and structural analyses of phospho-mimic CRMP2. Phosphorylation of CRMP2 undergoes small conformational changes at the C-terminal tail with shifting the surface charge, which not only alters the interactions within the CRMP2 tetramer but also alters the interactions with GTP-tubulin. Consequently, phospho-mimic CRMP2 fails to form a hetero-trimer with GTP-tubulin, thus losing the ability to establish and maintain the axonal microtubules.Key words: CRMP2, phosphorylation, microtubule, axon, crystal structure.	+
-		+
-	Structural Insights into the Altering Function of CRMP2 by Phosphorylation.,Sumi T, Imasaki T, Aoki M, Sakai N, Nitta E, Shirouzu M, Nitta R Cell Struct Funct. 2018;43(1):15-23. doi: 10.1247/csf.17025. PMID:29479005<ref>PMID:29479005</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5yzb" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Aoki, M]]	+	[[Category: Aoki M]]
-	[[Category: Imasaki, T]]	+	[[Category: Imasaki T]]
-	[[Category: Nitta, E]]	+	[[Category: Nitta E]]
-	[[Category: Nitta, R]]	+	[[Category: Nitta R]]
-	[[Category: Sakai, N]]	+	[[Category: Sakai N]]
-	[[Category: Shirouzu, M]]	+	[[Category: Shirouzu M]]
-	[[Category: Sumi, T]]	+	[[Category: Sumi T]]
-	~~[[Category: Collapsin response mediator protein]]~~	+
-	~~[[Category: Cytosolic protein]]~~	+
-	~~[[Category: Developmental protein]]~~	+
-	~~[[Category: Dihydropyrimidase-related protein]]~~	+
-	~~[[Category: Microtubule associated protein]]~~	+
-	~~[[Category: Neurogenesis]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 09:31, 21 October 2020

OCA — Wed, 21 Oct 2020 09:31:55 GMT

←Older revision		Revision as of 09:31, 21 October 2020
Line 1:		Line 1:

	==Crystal Structure of Human CRMP-2 with S522D-T509D-T514D-S518D mutations crystallized with GSK3b==		==Crystal Structure of Human CRMP-2 with S522D-T509D-T514D-S518D mutations crystallized with GSK3b==
-	<StructureSection load='5yzb' size='340' side='right' caption='[[5yzb]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='5yzb' size='340' side='right'caption='[[5yzb]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5yzb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZB OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5YZB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5yzb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YZB FirstGlance]. <br>
-	</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=5yzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzb OCA], [http://pdbe.org/5yzb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yzb RCSB], [http://www.ebi.ac.uk/pdbsum/5yzb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzb ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzb OCA], [http://pdbe.org/5yzb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yzb RCSB], [http://www.ebi.ac.uk/pdbsum/5yzb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzb ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Aoki, M]]		[[Category: Aoki, M]]
	[[Category: Imasaki, T]]		[[Category: Imasaki, T]]

OCA at 07:36, 21 March 2018

OCA — Wed, 21 Mar 2018 07:36:26 GMT

←Older revision		Revision as of 07:36, 21 March 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5yzb is ~~ON HOLD~~	+	==Crystal Structure of Human CRMP-2 with S522D-T509D-T514D-S518D mutations crystallized with GSK3b==
		+	<StructureSection load='5yzb' size='340' side='right' caption='[[5yzb]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5yzb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YZB FirstGlance]. <br>
		+	</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=5yzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzb OCA], [http://pdbe.org/5yzb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yzb RCSB], [http://www.ebi.ac.uk/pdbsum/5yzb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzb ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DPYL2_HUMAN DPYL2_HUMAN]] Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (By similarity). Plays a role in neuron projection morphogenesis.<ref>PMID:11477421</ref> <ref>PMID:15466863</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Collapsin response mediator protein 2 (CRMP2) regulates neuronal polarity by controlling microtubule dynamics. CRMP2 activity is regulated by semaphorin-induced phosphorylation at the C-terminal tail domain. Unphosphorylated CRMP2 induces effective axonal microtubule formation to give the axonal characteristics to a neurite, whereas phosphorylated CRMP2 leads to the apparently opposite effect, growth cone collapse. We have recently characterized the structural detail of CRMP2-induced axonal microtubule formation (Niwa et al. (2017) Sci. Rep., 7: 10681). CRMP2 forms the hetero-trimer with GTP-tubulin to induce effective axonal microtubule formation in the future axon. Phosphorylation of CRMP2 has been reported to decrease the affinity between CRMP2 and the microtubule, albeit the molecular mechanisms of how the phosphorylation of CRMP2 changes the structure to achieve distinct effects from unphosphorylated CRMP2 is not well understood. Here we performed a series of biochemical and structural analyses of phospho-mimic CRMP2. Phosphorylation of CRMP2 undergoes small conformational changes at the C-terminal tail with shifting the surface charge, which not only alters the interactions within the CRMP2 tetramer but also alters the interactions with GTP-tubulin. Consequently, phospho-mimic CRMP2 fails to form a hetero-trimer with GTP-tubulin, thus losing the ability to establish and maintain the axonal microtubules.Key words: CRMP2, phosphorylation, microtubule, axon, crystal structure.

-	~~Authors: Imasaki, T~~., Sumi, T., Aoki, M., Sakai, N., Nitta, E., Shirouzu, M., Nitta, R.	+	Structural Insights into the Altering Function of CRMP2 by Phosphorylation.,Sumi T, Imasaki T, Aoki M, Sakai N, Nitta E, Shirouzu M, Nitta R Cell Struct Funct. 2018;43(1):15-23. doi: 10.1247/csf.17025. PMID:29479005<ref>PMID:29479005</ref>

-	~~Description: Crystal Structure~~ of ~~Human CRMP~~-~~2 with S522D~~-~~S522D-T509D-T514D-S518D mutations crystallized with GSK3b~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 5yzb" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Aoki, M]]		[[Category: Aoki, M]]
	[[Category: Imasaki, T]]		[[Category: Imasaki, T]]
		+	[[Category: Nitta, E]]
	[[Category: Nitta, R]]		[[Category: Nitta, R]]
	[[Category: Sakai, N]]		[[Category: Sakai, N]]
	[[Category: Shirouzu, M]]		[[Category: Shirouzu, M]]
-	[[Category: Nitta, E]]
	[[Category: Sumi, T]]		[[Category: Sumi, T]]
		+	[[Category: Collapsin response mediator protein]]
		+	[[Category: Cytosolic protein]]
		+	[[Category: Developmental protein]]
		+	[[Category: Dihydropyrimidase-related protein]]
		+	[[Category: Microtubule associated protein]]
		+	[[Category: Neurogenesis]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Protein binding]]

OCA: Protected "5yzb" [edit=sysop:move=sysop]

OCA — Wed, 20 Dec 2017 04:53:08 GMT

Protected "5yzb" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:53, 20 December 2017

OCA: New page: '''Unreleased structure''' The entry 5yzb is ON HOLD Authors: Imasaki, T., Sumi, T., Aoki, M., Sakai, N., Nitta, E., Shirouzu, M., Nitta, R. Description: Crystal Structure of Human CRM...

OCA — Wed, 20 Dec 2017 04:53:07 GMT

New page: '''Unreleased structure''' The entry 5yzb is ON HOLD Authors: Imasaki, T., Sumi, T., Aoki, M., Sakai, N., Nitta, E., Shirouzu, M., Nitta, R. Description: Crystal Structure of Human CRM...

New page

'''Unreleased structure'''

The entry 5yzb is ON HOLD

Authors: Imasaki, T., Sumi, T., Aoki, M., Sakai, N., Nitta, E., Shirouzu, M., Nitta, R.

Description: Crystal Structure of Human CRMP-2 with S522D-S522D-T509D-T514D-S518D mutations crystallized with GSK3b
[[Category: Unreleased Structures]]
[[Category: Aoki, M]]
[[Category: Imasaki, T]]
[[Category: Nitta, R]]
[[Category: Sakai, N]]
[[Category: Shirouzu, M]]
[[Category: Nitta, E]]
[[Category: Sumi, T]]