This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1op4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1op4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1op4" /> '''Solution Structure of Neural Cadherin Prodom...)
Current revision (05:49, 17 April 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1op4.gif|left|200px]]<br /><applet load="1op4" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1op4" />
 
-
'''Solution Structure of Neural Cadherin Prodomain'''<br />
 
-
==Overview==
+
==Solution Structure of Neural Cadherin Prodomain==
-
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.
+
<StructureSection load='1op4' size='340' side='right'caption='[[1op4]]' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
 +
</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/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=1op4 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1OP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OP4 OCA].
+
*[[Cadherin 3D structures|Cadherin 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15130472 15130472]
+
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Single protein]]
+
[[Category: Colman DR]]
-
[[Category: Colman, D.R.]]
+
[[Category: Farooq A]]
-
[[Category: Farooq, A.]]
+
[[Category: Koch AW]]
-
[[Category: Koch, A.W.]]
+
[[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]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:04:49 2007''
+

Current revision

Solution Structure of Neural Cadherin Prodomain

PDB ID 1op4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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