1eg4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:02, 7 February 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1eg4.png|left|200px]]
 
-
{{STRUCTURE_1eg4| PDB=1eg4 | SCENE= }}
+
==STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE==
 +
<StructureSection load='1eg4' size='340' side='right'caption='[[1eg4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1eg4]] is a 2 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=1EG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EG4 FirstGlance]. <br>
 +
</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&#8491;</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=1eg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eg4 OCA], [https://pdbe.org/1eg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1eg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eg4 ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/DAG1_HUMAN DAG1_HUMAN] Defects in DAG1 are the cause of muscular dystrophy-dystroglycanopathy limb-girdle type C7 (MDDGC7) [MIM:[https://omim.org/entry/613818 613818]. An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with mental retardation without structural brain anomalies. Note=MDDGC7 is caused by DAG1 mutations that interfere with normal post-translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation.<ref>PMID:21388311</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DAG1_HUMAN DAG1_HUMAN] The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.<ref>PMID:9851927</ref> <ref>PMID:11724572</ref> <ref>PMID:16254364</ref> <ref>PMID:17360738</ref> Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for M.leprae in peripheral nerve Schwann cells but only in the presence of the G-domain of LAMA2, and for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.<ref>PMID:9851927</ref> <ref>PMID:11724572</ref> <ref>PMID:16254364</ref> <ref>PMID:17360738</ref> Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.<ref>PMID:9851927</ref> <ref>PMID:11724572</ref> <ref>PMID:16254364</ref> <ref>PMID:17360738</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/eg/1eg4_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=1eg4 ConSurf].
 +
<div style="clear:both"></div>
-
===STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE===
+
==See Also==
-
 
+
*[[Dystrophin|Dystrophin]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
[[1eg4]] is a 2 chain structure with sequence 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=1EG4 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
<ref group="xtra">PMID:010932245</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Eck, M J.]]
+
[[Category: Large Structures]]
-
[[Category: Huang, X.]]
+
[[Category: Eck MJ]]
-
[[Category: Joachimiak, A.]]
+
[[Category: Huang X]]
-
[[Category: Poy, F.]]
+
[[Category: Joachimiak A]]
-
[[Category: Sudol, M.]]
+
[[Category: Poy F]]
-
[[Category: Zhang, R.]]
+
[[Category: Sudol M]]
-
[[Category: Ef-hand like domain]]
+
[[Category: Zhang R]]
-
[[Category: Structural protein]]
+
-
[[Category: Ww domain]]
+

Current revision

STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE

PDB ID 1eg4

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/1eg4"
Personal tools