2dh3

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{{Seed}}
 
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[[Image:2dh3.png|left|200px]]
 
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==Crystal Structure of human ED-4F2hc==
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The line below this paragraph, containing "STRUCTURE_2dh3", creates the "Structure Box" on the page.
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<StructureSection load='2dh3' size='340' side='right'caption='[[2dh3]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2dh3]] 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=2DH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DH3 FirstGlance]. <br>
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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]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2dh3| PDB=2dh3 | SCENE= }}
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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=2dh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dh3 OCA], [https://pdbe.org/2dh3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dh3 RCSB], [https://www.ebi.ac.uk/pdbsum/2dh3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dh3 ProSAT]</span></td></tr>
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</table>
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===Crystal Structure of human ED-4F2hc===
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== Function ==
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[https://www.uniprot.org/uniprot/4F2_HUMAN 4F2_HUMAN] Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier.<ref>PMID:11557028</ref> <ref>PMID:9829974</ref> <ref>PMID:9751058</ref> <ref>PMID:9878049</ref> <ref>PMID:10903140</ref> <ref>PMID:11311135</ref> <ref>PMID:11389679</ref> <ref>PMID:11564694</ref> <ref>PMID:11742812</ref> <ref>PMID:12117417</ref> <ref>PMID:12225859</ref> <ref>PMID:14603368</ref> <ref>PMID:12716892</ref> <ref>PMID:15980244</ref> <ref>PMID:15769744</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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The line below this paragraph, {{ABSTRACT_PUBMED_17724034}}, adds the Publication Abstract to the page
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Check<jmol>
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(as it appears on PubMed at http://www.pubmed.gov), where 17724034 is the PubMed ID number.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dh/2dh3_consurf.spt"</scriptWhenChecked>
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{{ABSTRACT_PUBMED_17724034}}
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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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2DH3 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=2DH3 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=2dh3 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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The structure of human 4F2hc ectodomain provides a model for homodimerization and electrostatic interaction with plasma membrane., Fort J, de la Ballina LR, Burghardt HE, Ferrer-Costa C, Turnay J, Ferrer-Orta C, Uson I, Zorzano A, Fernandez-Recio J, Orozco M, Lizarbe MA, Fita I, Palacin M, J Biol Chem. 2007 Oct 26;282(43):31444-52. Epub 2007 Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17724034 17724034]
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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: Fita, I.]]
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[[Category: Fita I]]
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[[Category: Fort, J.]]
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[[Category: Fort J]]
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[[Category: Palacin, M.]]
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[[Category: Palacin M]]
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[[Category: Antiparallel beta-sheet]]
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[[Category: C-terminal domain]]
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[[Category: Coordination]]
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[[Category: Dimerization]]
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[[Category: Extracellular domain]]
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[[Category: Glycosidase like]]
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[[Category: Greek key]]
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[[Category: Signaling protein]]
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[[Category: Tim-barrel]]
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[[Category: Transport protein]]
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[[Category: Zn interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:28:08 2008''
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Current revision

Crystal Structure of human ED-4F2hc

PDB ID 2dh3

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