1o70

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:55, 10 April 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1o70.gif|left|200px]]
 
-
{{Structure
+
==Novel Fold Revealed by the Structure of a FAS1 Domain Pair from the Insect Cell Adhesion Molecule Fasciclin I==
-
|PDB= 1o70 |SIZE=350|CAPTION= <scene name='initialview01'>1o70</scene>, resolution 2.60&Aring;
+
<StructureSection load='1o70' size='340' side='right'caption='[[1o70]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+
<table><tr><td colspan='2'>[[1o70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O70 FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o70 OCA], [https://pdbe.org/1o70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o70 RCSB], [https://www.ebi.ac.uk/pdbsum/1o70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o70 ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o70 OCA], [http://www.ebi.ac.uk/pdbsum/1o70 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o70 RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/FAS1_DROME FAS1_DROME] Neural cell adhesion molecule.
-
 
+
== Evolutionary Conservation ==
-
'''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I'''
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==Overview==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o70_consurf.spt"</scriptWhenChecked>
-
Fasciclin I is an insect neural cell adhesion molecule consisting of four FAS1 domains, homologs of which are present in many bacterial, plant, and animal proteins. The crystal structure of FAS1 domains 3 and 4 of Drosophila fasciclin I reveals a novel domain fold, consisting of a seven-stranded beta wedge and a number of alpha helices. The two domains are arranged in a linear fashion and interact through a substantial polar interface. Missense mutations in the FAS1 domains of the human protein betaig-h3 cause corneal dystrophies. Many mutations alter highly conserved core residues, but the two most common mutations, affecting Arg-124 and Arg-555, map to exposed alpha-helical regions, suggesting reduced protein solubility as the disease mechanism.
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
 
+
<text>to colour the structure by Evolutionary Conservation</text>
-
==About this Structure==
+
</jmolCheckbox>
-
1O70 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O70 OCA].
+
</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=1o70 ConSurf].
-
 
+
<div style="clear:both"></div>
-
==Reference==
+
__TOC__
-
Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I., Clout NJ, Tisi D, Hohenester E, Structure. 2003 Feb;11(2):197-203. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12575939 12575939]
+
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Clout, N J.]]
+
[[Category: Clout NJ]]
-
[[Category: Hohenester, E.]]
+
[[Category: Hohenester E]]
-
[[Category: Tisi, D.]]
+
[[Category: Tisi D]]
-
[[Category: axon guidance]]
+
-
[[Category: cell adhesion]]
+
-
[[Category: corneal dystrophy]]
+
-
[[Category: extracellular module]]
+
-
[[Category: genetic disorder]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:40:46 2008''
+

Current revision

Novel Fold Revealed by the Structure of a FAS1 Domain Pair from the Insect Cell Adhesion Molecule Fasciclin I

PDB ID 1o70

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools