1r0d: Difference between revisions

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==HIP1R THATCH DOMAIN CORE==
==HIP1R THATCH DOMAIN CORE==
<StructureSection load='1r0d' size='340' side='right' caption='[[1r0d]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1r0d' size='340' side='right'caption='[[1r0d]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1r0d]] is a 8 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R0D FirstGlance]. <br>
<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>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</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>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HIP1R, HIP12, KIAA0655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<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>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1r0d RCSB], [http://www.ebi.ac.uk/pdbsum/1r0d PDBsum], [http://www.topsan.org/Proteins/MCSG/1r0d TOPSAN]</span></td></tr>
<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>
<table>
</table>
== Function ==
[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>  
== 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/r0/1r0d_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/1r0d_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/chain_selection.php?pdb_ID=2ata ConSurf].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:16415883<ref>PMID:16415883</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Brett, T J.]]
[[Category: Large Structures]]
[[Category: Fremont, D H.]]
[[Category: Brett TJ]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Fremont DH]]
[[Category: Actin-binding]]
[[Category: Endocytosis]]
[[Category: Mcsg]]
[[Category: Midwest center for structural genomic]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[Category: Structural protein]]

Latest revision as of 09:08, 17 April 2024

HIP1R THATCH DOMAIN COREHIP1R THATCH DOMAIN CORE

Structural highlights

1r0d is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Legendre-Guillemin V, Metzler M, Charbonneau M, Gan L, Chopra V, Philie J, Hayden MR, McPherson PS. HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain. J Biol Chem. 2002 May 31;277(22):19897-904. Epub 2002 Mar 11. PMID:11889126 doi:10.1074/jbc.M112310200
  2. ↑ Hyun TS, Rao DS, Saint-Dic D, Michael LE, Kumar PD, Bradley SV, Mizukami IF, Oravecz-Wilson KI, Ross TS. HIP1 and HIP1r stabilize receptor tyrosine kinases and bind 3-phosphoinositides via epsin N-terminal homology domains. J Biol Chem. 2004 Apr 2;279(14):14294-306. Epub 2004 Jan 19. PMID:14732715 doi:10.1074/jbc.M312645200

1r0d, resolution 1.90Å

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