4ihk: Difference between revisions

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'''Unreleased structure'''


The entry 4ihk is ON HOLD
==Crystal structure of the Collagen VI alpha3 N5 domain R1061Q==
<StructureSection load='4ihk' size='340' side='right'caption='[[4ihk]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ihk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IHK 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]] 1.2&#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=4ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihk OCA], [https://pdbe.org/4ihk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ihk RCSB], [https://www.ebi.ac.uk/pdbsum/4ihk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E9PWQ3_MOUSE E9PWQ3_MOUSE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Von Willebrand factor A (VWA) domains are versatile protein interaction domains with N and C termini in close proximity placing spatial constraints on overall protein structure. The 1.2 A crystal structures of a collagen VI VWA domain and a disease-causing point mutant show C-terminal extensions that place the N and C termini at opposite ends. This allows a "beads-on-a-string" arrangement of multiple VWA domains as observed for ten N-terminal domains of the collagen VI alpha3 chain. The extension is linked to the core domain by a salt bridge and two hydrophobic patches. Comparison of the wild-type and a muscular dystrophy-associated mutant structure identifies a potential perturbation of a protein interaction interface and indeed, the secretion of mutant collagen VI tetramers is affected. Homology modeling is used to locate a number of disease-associated mutations and analyze their structural impact, which will allow mechanistic analysis of collagen-VI-associated muscular dystrophy phenotypes.


Authors: Mikolajek, H., Becker, A-K.A., Paulsson, M. , Wagener, R., Werner, J.M.
A structure of a collagen VI VWA domain displays N and C termini at opposite sides of the protein.,Becker AK, Mikolajek H, Paulsson M, Wagener R, Werner JM Structure. 2014 Feb 4;22(2):199-208. doi: 10.1016/j.str.2013.06.028. Epub 2013, Dec 12. PMID:24332716<ref>PMID:24332716</ref>


Description: Crystal structure of the Collagen VI alpha3 N5 domain R1064Q
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ihk" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Collagen 3D structures|Collagen 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Becker AKA]]
[[Category: Mikolajek H]]
[[Category: Paulsson M]]
[[Category: Wagener R]]
[[Category: Werner JM]]
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