3l2j

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:06, 6 November 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3l2j.png|left|200px]]
 
-
<!--
+
==Dimeric structure of the ligand-free extracellular domain of the human parathyroid hormone receptor (PTH1R)==
-
The line below this paragraph, containing "STRUCTURE_3l2j", creates the "Structure Box" on the page.
+
<StructureSection load='3l2j' size='340' side='right'caption='[[3l2j]], [[Resolution|resolution]] 3.24&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'>[[3l2j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L2J 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]] 3.24&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
-
{{STRUCTURE_3l2j| PDB=3l2j | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l2j OCA], [https://pdbe.org/3l2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l2j RCSB], [https://www.ebi.ac.uk/pdbsum/3l2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l2j ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/PTH1R_HUMAN PTH1R_HUMAN] Blomstrand lethal chondrodysplasia;Dental ankylosis;Eiken syndrome;Metaphyseal chondrodysplasia, Jansen type;Enchondromatosis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease may be caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/PTH1R_HUMAN PTH1R_HUMAN] This is a receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system.<ref>PMID:18611381</ref> <ref>PMID:20172855</ref>
 +
== 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/l2/3l2j_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3l2j ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The parathyroid hormone receptor (PTH1R) is a class B G protein-coupled receptor that is activated by parathyroid hormone (PTH) and PTH-related protein (PTHrP). Little is known about the oligomeric state of the receptor and its regulation by hormone. The crystal structure of the ligand-free PTH1R extracellular domain (ECD) reveals an unexpected dimer in which the C-terminal segment of both ECD protomers forms an alpha-helix that mimics PTH/PTHrP by occupying the peptide binding groove of the opposing protomer. ECD-mediated oligomerization of intact PTH1R was confirmed in living cells by bioluminescence and fluorescence resonance energy transfer experiments. As predicted by the structure, PTH binding disrupted receptor oligomerization. A receptor rendered monomeric by mutations in the ECD retained wild-type PTH binding and cAMP signaling ability. Our results are consistent with the hypothesis that PTH1R forms constitutive dimers that are dissociated by ligand binding and that monomeric PTH1R is capable of activating G protein.
-
===Dimeric structure of the ligand-free extracellular domain of the human parathyroid hormone receptor (PTH1R)===
+
Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation.,Pioszak AA, Harikumar KG, Parker NR, Miller LJ, Xu HE J Biol Chem. 2010 Apr 16;285(16):12435-44. Epub 2010 Feb 19. PMID:20172855<ref>PMID:20172855</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_20172855}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 3l2j" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 20172855 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_20172855}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Escherichia coli K-12]]
-
3L2J is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli,_homo_sapiens Escherichia coli, homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L2J OCA].
+
[[Category: Homo sapiens]]
-
 
+
[[Category: Large Structures]]
-
==Reference==
+
[[Category: Pioszak AA]]
-
<ref group="xtra">PMID:20172855</ref><references group="xtra"/>
+
[[Category: Xu HE]]
-
[[Category: Escherichia coli, homo sapiens]]
+
-
[[Category: Pioszak, A A.]]
+
-
[[Category: Xu, H E.]]
+
-
[[Category: Cell membrane]]
+
-
[[Category: Dimer]]
+
-
[[Category: Disease mutation]]
+
-
[[Category: Disulfide bond]]
+
-
[[Category: Dwarfism]]
+
-
[[Category: Extracellular domain]]
+
-
[[Category: G-protein coupled receptor]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Mbp fusion protein]]
+
-
[[Category: Membrane]]
+
-
[[Category: Membrane protein]]
+
-
[[Category: Periplasm]]
+
-
[[Category: Receptor]]
+
-
[[Category: Sugar transport]]
+
-
[[Category: Transducer]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Transport]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 28 10:57:28 2010''
+

Current revision

Dimeric structure of the ligand-free extracellular domain of the human parathyroid hormone receptor (PTH1R)

PDB ID 3l2j

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3l2j"
Personal tools