1bhd: Difference between revisions
No edit summary |
No edit summary |
||
(4 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN== | ==SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN== | ||
<StructureSection load='1bhd' size='340' side='right' caption='[[1bhd]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1bhd' size='340' side='right'caption='[[1bhd]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bhd]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1bhd]] 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=1BHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhd OCA], [https://pdbe.org/1bhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bhd RCSB], [https://www.ebi.ac.uk/pdbsum/1bhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bhd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/UTRN_HUMAN UTRN_HUMAN] May play a role in anchoring the cytoskeleton to the plasma membrane. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bhd_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bhd_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1bhd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Line 31: | Line 32: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Keep NH]] | ||
[[Category: | [[Category: Kendrick-Jones J]] | ||
[[Category: | [[Category: Winder SJ]] | ||
Latest revision as of 14:01, 2 August 2023
SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHINSECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN
Structural highlights
FunctionUTRN_HUMAN May play a role in anchoring the cytoskeleton to the plasma membrane. 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 PubMedUtrophin is a close homologue of dystrophin, the protein defective in Duchenne muscular dystrophy. Like dystrophin, it is composed of three regions: an N-terminal region that binds actin filaments, a large central region with triple coiled-coil repeats, and a C-terminal region that interacts with components in the dystroglycan protein complex at the plasma membrane. The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin-binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin. Here, we present the 2.0 A structure of the second calponin homology domain of utrophin solved by X-ray crystallography, and compare it to the other calponin homology domains previously determined from spectrin and fimbrin. The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin.,Keep NH, Norwood FL, Moores CA, Winder SJ, Kendrick-Jones J J Mol Biol. 1999 Jan 22;285(3):1257-64. PMID:9887274[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|