1op4

From Proteopedia

(Difference between revisions)

Current revision

Solution Structure of Neural Cadherin Prodomain

Structural highlights

1op4 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 1 model
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CADH2_MOUSE Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.^[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

Classical cadherins mediate cell-cell adhesion through calcium-dependent homophilic interactions and are activated through cleavage of a prosequence in the late Golgi. We present here the first three-dimensional structure of a classical cadherin prosequence, solved by NMR. The prototypic prosequence of N-cadherin consists of an Ig-like domain and an unstructured C-terminal region. The folded part of the prosequence-termed prodomain-has a striking structural resemblance to cadherin "adhesive" domains that could not have been predicted from the amino acid sequence due to low sequence similarities. Our detailed structural and evolutionary analysis revealed that prodomains are distant relatives of cadherin "adhesive" domains but lack all the features known to be important for cadherin-cadherin interactions. The presence of an additional "nonadhesive" domain seems to make it impossible to engage homophilic interactions between cadherins that are necessary to activate adhesion, thus explaining the inactive state of prodomain-bearing cadherins.

Structure of the neural (N-) cadherin prodomain reveals a cadherin extracellular domain-like fold without adhesive characteristics.,Koch AW, Farooq A, Shan W, Zeng L, Colman DR, Zhou MM Structure. 2004 May;12(5):793-805. PMID:15130472^[3]

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

References

↑ Cavallaro U, Niedermeyer J, Fuxa M, Christofori G. N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling. Nat Cell Biol. 2001 Jul;3(7):650-7. PMID:11433297 doi:http://dx.doi.org/10.1038/35083041
↑ Yasuda S, Tanaka H, Sugiura H, Okamura K, Sakaguchi T, Tran U, Takemiya T, Mizoguchi A, Yagita Y, Sakurai T, De Robertis EM, Yamagata K. Activity-induced protocadherin arcadlin regulates dendritic spine number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases. Neuron. 2007 Nov 8;56(3):456-71. PMID:17988630 doi:http://dx.doi.org/10.1016/j.neuron.2007.08.020
↑ Koch AW, Farooq A, Shan W, Zeng L, Colman DR, Zhou MM. Structure of the neural (N-) cadherin prodomain reveals a cadherin extracellular domain-like fold without adhesive characteristics. Structure. 2004 May;12(5):793-805. PMID:15130472 doi:10.1016/j.str.2004.02.034

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1op4"

@@ Line 1: / Line 1: @@
-[[Image:1op4.png|left|200px]]
-<!--
+==Solution Structure of Neural Cadherin Prodomain==
-The line below this paragraph, containing "STRUCTURE_1op4", creates the "Structure Box" on the page.
+<StructureSection load='1op4' size='340' side='right'caption='[[1op4]]' 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'>[[1op4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OP4 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">Solution NMR, 1 model</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=1op4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1op4 OCA], [https://pdbe.org/1op4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1op4 RCSB], [https://www.ebi.ac.uk/pdbsum/1op4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1op4 ProSAT]</span></td></tr>
-{{STRUCTURE_1op4|  PDB=1op4  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CADH2_MOUSE CADH2_MOUSE] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.<ref>PMID:11433297</ref> <ref>PMID:17988630</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/op/1op4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1op4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Classical cadherins mediate cell-cell adhesion through calcium-dependent homophilic interactions and are activated through cleavage of a prosequence in the late Golgi. We present here the first three-dimensional structure of a classical cadherin prosequence, solved by NMR. The prototypic prosequence of N-cadherin consists of an Ig-like domain and an unstructured C-terminal region. The folded part of the prosequence-termed prodomain-has a striking structural resemblance to cadherin "adhesive" domains that could not have been predicted from the amino acid sequence due to low sequence similarities. Our detailed structural and evolutionary analysis revealed that prodomains are distant relatives of cadherin "adhesive" domains but lack all the features known to be important for cadherin-cadherin interactions. The presence of an additional "nonadhesive" domain seems to make it impossible to engage homophilic interactions between cadherins that are necessary to activate adhesion, thus explaining the inactive state of prodomain-bearing cadherins.
-===Solution Structure of Neural Cadherin Prodomain===
+Structure of the neural (N-) cadherin prodomain reveals a cadherin extracellular domain-like fold without adhesive characteristics.,Koch AW, Farooq A, Shan W, Zeng L, Colman DR, Zhou MM Structure. 2004 May;12(5):793-805. PMID:15130472<ref>PMID:15130472</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_15130472}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1op4" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15130472 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_15130472}}
-==About this Structure==
-[[1op4]] is a 1 chain structure of [[Cadherin]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OP4 OCA].
 ==See Also==
-*[[Cadherin]]
+*[[Cadherin 3D structures|Cadherin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:15130472</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Colman, D R.]]
+[[Category: Colman DR]]
-[[Category: Farooq, A.]]
+[[Category: Farooq A]]
-[[Category: Koch, A W.]]
+[[Category: Koch AW]]
-[[Category: Shan, W.]]
+[[Category: Shan W]]
-[[Category: Zeng, L.]]
+[[Category: Zeng L]]
-[[Category: Zhou, M M.]]
+[[Category: Zhou M-M]]
-[[Category: Beta sandwich]]
-[[Category: Cadherin-like domain]]
-[[Category: Cell adhesion]]

1op4

From Proteopedia

Current revision

Solution Structure of Neural Cadherin Prodomain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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