1c9l: Difference between revisions

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{{Seed}}
[[Image:1c9l.png|left|200px]]


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==PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN==
The line below this paragraph, containing "STRUCTURE_1c9l", creates the "Structure Box" on the page.
<StructureSection load='1c9l' size='340' side='right'caption='[[1c9l]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1c9l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9L FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9l OCA], [https://pdbe.org/1c9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9l RCSB], [https://www.ebi.ac.uk/pdbsum/1c9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9l ProSAT]</span></td></tr>
{{STRUCTURE_1c9l| PDB=1c9l |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/CLH1_RAT CLH1_RAT] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.
== 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/c9/1c9l_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=1c9l ConSurf].
<div style="clear:both"></div>


===PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN===
==See Also==
 
*[[Clathrin 3D structures|Clathrin 3D structures]]
 
__TOC__
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</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_10655490}}, adds the Publication Abstract to the page
[[Category: Homo sapiens]]
(as it appears on PubMed at http://www.pubmed.gov), where 10655490 is the PubMed ID number.
[[Category: Large Structures]]
-->
{{ABSTRACT_PUBMED_10655490}}
 
==About this Structure==
1C9L is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9L OCA].
 
==Reference==
<ref group="xtra">PMID:10655490</ref><references group="xtra"/>
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Haar, E ter.]]
[[Category: Harrison SC]]
[[Category: Harrison, S C.]]
[[Category: Kirchhausen T]]
[[Category: Kirchhausen, T.]]
[[Category: Ter Haar E]]
[[Category: Beta-propeller]]
[[Category: Helical hairpin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 15:14:09 2009''

Latest revision as of 06:41, 7 February 2024

PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN

1c9l, resolution 2.90Å

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