View source for 3lvh


==Crystal structure of a clathrin heavy chain and clathrin light chain complex==
<StructureSection load='3lvh' size='340' side='right' caption='[[3lvh]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lvh]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LVH FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lvg|3lvg]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLTC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN]), CLTB, CLTLB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=3lvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lvh OCA], [http://pdbe.org/3lvh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lvh RCSB], [http://www.ebi.ac.uk/pdbsum/3lvh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lvh ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CLH1_BOVIN CLH1_BOVIN]] 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. [[http://www.uniprot.org/uniprot/CLCB_BOVIN CLCB_BOVIN]] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. 
== 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/lv/3lvh_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=3lvh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Clathrin-coated vesicle formation is responsible for membrane traffic to and from the endocytic pathway during receptor-mediated endocytosis and organelle biogenesis, influencing how cells relate to their environment. Generating these vesicles involves self-assembly of clathrin molecules into a latticed coat on membranes that recruits receptors and organizes protein machinery necessary for budding. Here we define a molecular mechanism regulating clathrin lattice formation by obtaining structural information from co-crystals of clathrin subunits. Low resolution X-ray diffraction data (7.9-9.0 A) was analyzed using a combination of molecular replacement with an energy-minimized model and noncrystallographic symmetry averaging. Resulting topological information revealed two conformations of the regulatory clathrin light chain bound to clathrin heavy chain. Based on protein domain positions, mutagenesis, and biochemical assays, we identify an electrostatic interaction between the clathrin subunits that allows the observed conformational variation in clathrin light chains to alter the conformation of the clathrin heavy chain and thereby regulates assembly.

Conformation switching of clathrin light chain regulates clathrin lattice assembly.,Wilbur JD, Hwang PK, Ybe JA, Lane M, Sellers BD, Jacobson MP, Fletterick RJ, Brodsky FM Dev Cell. 2010 May 18;18(5):841-8. PMID:20493816<ref>PMID:20493816</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lvh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Clathrin|Clathrin]]
*[[Temperature color schemes|Temperature color schemes]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bovin]]
[[Category: Brodsky, F M]]
[[Category: Fletterick, R J]]
[[Category: Hwang, P K]]
[[Category: Jacobson, M P]]
[[Category: Lane, M]]
[[Category: Sellers, B D]]
[[Category: Wilbur, J D]]
[[Category: Ybe, J A]]
[[Category: Coated pit]]
[[Category: Cytoplasmic vesicle]]
[[Category: Membrane]]
[[Category: Self assembly]]
[[Category: Structural protein]]