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1r0d

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[[Image:1r0d.gif|left|200px]]
 
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{{Structure
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==HIP1R THATCH DOMAIN CORE==
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|PDB= 1r0d |SIZE=350|CAPTION= <scene name='initialview01'>1r0d</scene>, resolution 1.90&Aring;
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<StructureSection load='1r0d' size='340' side='right'caption='[[1r0d]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1r0d]] is a 8 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=1R0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R0D FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE= HIP1R, HIP12, KIAA0655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01608 I_LWEQ]</span>
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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=1r0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0d OCA], [https://pdbe.org/1r0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r0d RCSB], [https://www.ebi.ac.uk/pdbsum/1r0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r0d ProSAT], [https://www.topsan.org/Proteins/MCSG/1r0d TOPSAN]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0d OCA], [http://www.ebi.ac.uk/pdbsum/1r0d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r0d RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HIP1R_HUMAN HIP1R_HUMAN] Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis.<ref>PMID:11889126</ref> <ref>PMID:14732715</ref>
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== Evolutionary Conservation ==
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'''HIP1R THATCH DOMAIN CORE'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/1r0d_consurf.spt"</scriptWhenChecked>
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Huntingtin-interacting protein-1 related (HIP1R) has a crucial protein-trafficking role, mediating associations between actin and clathrin-coated structures at the plasma membrane and trans-Golgi network. Here, we characterize the F-actin-binding region of HIP1R, termed the talin-HIP1/R/Sla2p actin-tethering C-terminal homology (THATCH) domain. The 1.9-A crystal structure of the human HIP1R THATCH core reveals a large sequence-conserved surface patch created primarily by residues from the third and fourth helices of a unique five-helix bundle. Point mutations of seven contiguous patch residues produced significant decreases in F-actin binding. We also show that THATCH domains have a conserved C-terminal latch capable of oligomerizing the core, thereby modulating F-actin engagement. Collectively, these results establish a framework for investigating the links between endocytosis and actin dynamics mediated by THATCH domain-containing proteins.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1R0D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0D OCA].
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</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=1r0d ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Structural definition of the F-actin-binding THATCH domain from HIP1R., Brett TJ, Legendre-Guillemin V, McPherson PS, Fremont DH, Nat Struct Mol Biol. 2006 Feb;13(2):121-30. Epub 2006 Jan 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16415883 16415883]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brett, T J.]]
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[[Category: Brett TJ]]
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[[Category: Fremont, D H.]]
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[[Category: Fremont DH]]
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[[Category: MCSG, Midwest Center for Structural Genomics.]]
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[[Category: actin-binding]]
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[[Category: endocytosis]]
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[[Category: mcsg]]
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[[Category: midwest center for structural genomic]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:26 2008''
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Current revision

HIP1R THATCH DOMAIN CORE

PDB ID 1r0d

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