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1qag

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Revision as of 08:12, 24 February 2018

Actin binding region of the dystrophin homologue utrophin

Structural highlights

1qag is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UTRO_HUMAN] May play a role in anchoring the cytoskeleton to the plasma membrane (By similarity).

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

BACKGROUND: Utrophin is a large multidomain protein that belongs to a superfamily of actin-binding proteins, which includes dystrophin, alpha-actinin, beta-spectrin, fimbrin, filamin and plectin. All the members of this family contain a common actin-binding region at their N termini and perform a wide variety of roles associated with the actin cytoskeleton. Utrophin is the autosomal homologue of dystrophin, the protein defective in the X-linked Duchenne and Becker muscular dystrophies, and upregulation of utrophin has been suggested as a potential therapy for muscular dystrophy patients. RESULTS: The structure of the actin-binding region of utrophin, consisting of two calponin-homology (CH) domains, has been solved at 3.0 A resolution. It is composed of an antiparallel dimer with each of the monomers being present in an extended dumbell shape and the two CH domains being separated by a long central helix. This extended conformation is in sharp contrast to the compact monomer structure of the N-terminal actin-binding region of fimbrin. CONCLUSIONS: The crystal structure of the actin-binding region of utrophin suggests that these actin-binding domains may be more flexible than was previously thought and that this flexibility may allow domain reorganisation and play a role in the actin-binding mechanism. Thus utrophin could possibly bind to actin in an extended conformation so that the sites previously identified as being important for actin binding may be directly involved in this interaction.

Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer.,Keep NH, Winder SJ, Moores CA, Walke S, Norwood FL, Kendrick-Jones J Structure. 1999 Dec 15;7(12):1539-46. PMID:10647184^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Keep NH, Winder SJ, Moores CA, Walke S, Norwood FL, Kendrick-Jones J. Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer. Structure. 1999 Dec 15;7(12):1539-46. PMID:10647184

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qag"

@@ Line 1: / Line 1: @@
 ==Actin binding region of the dystrophin homologue utrophin==
 <StructureSection load='1qag' size='340' side='right' caption='[[1qag]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1qag]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QAG FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qag OCA], [http://pdbe.org/1qag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qag RCSB], [http://www.ebi.ac.uk/pdbsum/1qag PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qag OCA], [http://pdbe.org/1qag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qag RCSB], [http://www.ebi.ac.uk/pdbsum/1qag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qag ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qa/1qag_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qa/1qag_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1qag

From Proteopedia

Revision as of 08:12, 24 February 2018

Actin binding region of the dystrophin homologue utrophin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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