|
|
| (15 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:1op4.gif|left|200px]] | |
| | | | |
| - | {{Structure
| + | ==Solution Structure of Neural Cadherin Prodomain== |
| - | |PDB= 1op4 |SIZE=350|CAPTION= <scene name='initialview01'>1op4</scene>
| + | <StructureSection load='1op4' size='340' side='right'caption='[[1op4]]' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <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> |
| - | |ACTIVITY=
| + | </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> |
| - | |GENE= CDH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
| + | <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> |
| - | |DOMAIN=
| + | </table> |
| - | |RELATEDENTRY= | + | == Function == |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1op4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1op4 OCA], [http://www.ebi.ac.uk/pdbsum/1op4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1op4 RCSB]</span>
| + | [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®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 1op4" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | 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.
| + | *[[Cadherin 3D structures|Cadherin 3D structures]] |
| - | | + | == References == |
| - | ==About this Structure==
| + | <references/> |
| - | 1OP4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OP4 OCA].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==Reference== | + | [[Category: Large Structures]] |
| - | 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://www.ncbi.nlm.nih.gov/pubmed/15130472 15130472]
| + | |
| | [[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://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:25 2008''
| + | |
| Structural highlights
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.
See Also
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
|
