2vm8

From Proteopedia

(Difference between revisions)

Current revision

Human CRMP-2 crystallised in the presence of Mg

Structural highlights

2vm8 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The collapsin response mediator protein 2 (CRMP-2) is a central molecule regulating axonal growth cone guidance. It interacts with the cytoskeleton and mediates signals related to myelin-induced axonal growth inhibition. CRMP-2 has also been characterized as a constituent of neurofibrillary tangles in Alzheimer's disease. CD spectroscopy and thermal stability assays using the Thermofluor method indicated that Ca2+ and Mg2+ affect the stability of CRMP-2 and prevent the formation of beta-aggregates upon heating. Gel filtration showed that the presence of Ca2+ or Mg2+ promoted the formation of CRMP-2 homotetramers, and this was further proven by small-angle X-ray scattering experiments, where a 3D solution structure for CRMP-2 was obtained. Previously, we described a crystal structure of human CRMP-2 complexed with calcium. In the present study, we determined the structure of CRMP-2 in the absence of calcium at 1.9 A resolution. When Ca2+ was omitted, crystals could only be grown in the presence of Mg2+ ions. By a proteomic approach, we further identified a number of post-translational modifications in CRMP-2 from rat brain hippocampus and mapped them onto the crystal structure.

Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2.,Majava V, Loytynoja N, Chen WQ, Lubec G, Kursula P FEBS J. 2008 Sep;275(18):4583-96. Epub 2008 Aug 11. PMID:18699782^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Inagaki N, Chihara K, Arimura N, Menager C, Kawano Y, Matsuo N, Nishimura T, Amano M, Kaibuchi K. CRMP-2 induces axons in cultured hippocampal neurons. Nat Neurosci. 2001 Aug;4(8):781-2. PMID:11477421 doi:http://dx.doi.org/10.1038/90476
↑ Cole AR, Knebel A, Morrice NA, Robertson LA, Irving AJ, Connolly CN, Sutherland C. GSK-3 phosphorylation of the Alzheimer epitope within collapsin response mediator proteins regulates axon elongation in primary neurons. J Biol Chem. 2004 Nov 26;279(48):50176-80. Epub 2004 Oct 5. PMID:15466863 doi:http://dx.doi.org/10.1074/jbc.C400412200
↑ Majava V, Loytynoja N, Chen WQ, Lubec G, Kursula P. Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2. FEBS J. 2008 Sep;275(18):4583-96. Epub 2008 Aug 11. PMID:18699782 doi:10.1111/j.1742-4658.2008.06601.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vm8"

Categories: Homo sapiens | Large Structures | Kursula P

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2vm8.png|left|200px]]
-<!--
+==Human CRMP-2 crystallised in the presence of Mg==
-The line below this paragraph, containing "STRUCTURE_2vm8", creates the "Structure Box" on the page.
+<StructureSection load='2vm8' size='340' side='right'caption='[[2vm8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2vm8]] 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=2VM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VM8 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_2vm8|  PDB=2vm8  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vm8 OCA], [https://pdbe.org/2vm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vm8 RCSB], [https://www.ebi.ac.uk/pdbsum/2vm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vm8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/2vm8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vm8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The collapsin response mediator protein 2 (CRMP-2) is a central molecule regulating axonal growth cone guidance. It interacts with the cytoskeleton and mediates signals related to myelin-induced axonal growth inhibition. CRMP-2 has also been characterized as a constituent of neurofibrillary tangles in Alzheimer's disease. CD spectroscopy and thermal stability assays using the Thermofluor method indicated that Ca2+ and Mg2+ affect the stability of CRMP-2 and prevent the formation of beta-aggregates upon heating. Gel filtration showed that the presence of Ca2+ or Mg2+ promoted the formation of CRMP-2 homotetramers, and this was further proven by small-angle X-ray scattering experiments, where a 3D solution structure for CRMP-2 was obtained. Previously, we described a crystal structure of human CRMP-2 complexed with calcium. In the present study, we determined the structure of CRMP-2 in the absence of calcium at 1.9 A resolution. When Ca2+ was omitted, crystals could only be grown in the presence of Mg2+ ions. By a proteomic approach, we further identified a number of post-translational modifications in CRMP-2 from rat brain hippocampus and mapped them onto the crystal structure.
-===HUMAN CRMP-2 CRYSTALLISED IN THE PRESENCE OF MG===
+Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2.,Majava V, Loytynoja N, Chen WQ, Lubec G, Kursula P FEBS J. 2008 Sep;275(18):4583-96. Epub 2008 Aug 11. PMID:18699782<ref>PMID:18699782</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_18699782}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2vm8" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 18699782 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18699782}}
+__TOC__
+</StructureSection>
-==About this Structure==
-VM8 is a 4 chains structure of sequences 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=2VM8 OCA].
-==Reference==
-<ref group="xtra">PMID:18699782</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Kursula, P.]]
+[[Category: Large Structures]]
-[[Category: Axonal pathfinding]]
+[[Category: Kursula P]]
-[[Category: Crmp]]
-[[Category: Cytoplasm]]
-[[Category: Developmental protein]]
-[[Category: Differentiation]]
-[[Category: Neurogenesis]]
-[[Category: Phosphoprotein]]
-[[Category: Polymorphism]]
-[[Category: Signaling protein]]
-[[Category: Tim barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:19:26 2009''

2vm8

From Proteopedia

Current revision

Human CRMP-2 crystallised in the presence of Mg

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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