1et3: Difference between revisions

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{{Theoretical_model}}
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[[Image:1et3.png|left|200px]]


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==MOLECULAR MODEL OF PTHRP (1-34) IN COMPLEX WITH THE PTH/PTHRP RECEPTOR (PTHR1).==
The line below this paragraph, containing "STRUCTURE_1et3", creates the "Structure Box" on the page.
<StructureSection load='1et3' size='340' side='right'caption='[[1et3]]' 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'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ET3 FirstGlance]. <br>
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</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=1et3 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1et3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1et3 ProSAT]</span></td></tr>
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</table>
{{STRUCTURE_1et3|  PDB=1et3  |  SCENE=  }}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-terminal fragment 1-34 of parathyroid hormone (PTH), administered intermittently, results in increased bone formation in patients with osteoporosis. PTH and a related molecule, parathyroid hormone-related peptide (PTHrP), act on cells via a common PTH/PTHrP receptor. To define more precisely the ligand-receptor interactions, we have crystallized human PTH (hPTH)-(1-34) and determined the structure to 0.9-A resolution. hPTH-(1-34) crystallizes as a slightly bent, long helical dimer. Analysis reveals that the extended helical conformation of hPTH-(1-34) is the likely bioactive conformation. We have developed molecular models for the interaction of hPTH-(1-34) and hPTHrP-(1-34) with the PTH/PTHrP receptor. A receptor binding pocket for the N terminus of hPTH-(1-34) and a hydrophobic interface with the receptor for the C terminus of hPTH-(1-34) are proposed.


===MOLECULAR MODEL OF PTHRP (1-34) IN COMPLEX WITH THE PTH/PTHRP RECEPTOR (PTHR1).===
Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution.,Jin L, Briggs SL, Chandrasekhar S, Chirgadze NY, Clawson DK, Schevitz RW, Smiley DL, Tashjian AH, Zhang F J Biol Chem. 2000 Sep 1;275(35):27238-44. PMID:10837469<ref>PMID:10837469</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 10837469 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_10837469}}
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</StructureSection>
==About this Structure==
[[Category: Theoretical Model]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ET3 OCA].
[[Category: Large Structures]]
 
==Reference==
<ref group="xtra">PMID:10837469</ref><references group="xtra"/>
[[Category: Briggs, S L]]
[[Category: Briggs, S L]]
[[Category: Chandrasekhar, S]]
[[Category: Chandrasekhar, S]]
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[[Category: Tashjian, A H]]
[[Category: Tashjian, A H]]
[[Category: Zhang, F]]
[[Category: Zhang, F]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 08:43:20 2010''

Latest revision as of 12:41, 21 July 2021

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MOLECULAR MODEL OF PTHRP (1-34) IN COMPLEX WITH THE PTH/PTHRP RECEPTOR (PTHR1).MOLECULAR MODEL OF PTHRP (1-34) IN COMPLEX WITH THE PTH/PTHRP RECEPTOR (PTHR1).

Structural highlights

For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, PDBsum, ProSAT

Publication Abstract from PubMed

The N-terminal fragment 1-34 of parathyroid hormone (PTH), administered intermittently, results in increased bone formation in patients with osteoporosis. PTH and a related molecule, parathyroid hormone-related peptide (PTHrP), act on cells via a common PTH/PTHrP receptor. To define more precisely the ligand-receptor interactions, we have crystallized human PTH (hPTH)-(1-34) and determined the structure to 0.9-A resolution. hPTH-(1-34) crystallizes as a slightly bent, long helical dimer. Analysis reveals that the extended helical conformation of hPTH-(1-34) is the likely bioactive conformation. We have developed molecular models for the interaction of hPTH-(1-34) and hPTHrP-(1-34) with the PTH/PTHrP receptor. A receptor binding pocket for the N terminus of hPTH-(1-34) and a hydrophobic interface with the receptor for the C terminus of hPTH-(1-34) are proposed.

Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution.,Jin L, Briggs SL, Chandrasekhar S, Chirgadze NY, Clawson DK, Schevitz RW, Smiley DL, Tashjian AH, Zhang F J Biol Chem. 2000 Sep 1;275(35):27238-44. PMID:10837469[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Jin L, Briggs SL, Chandrasekhar S, Chirgadze NY, Clawson DK, Schevitz RW, Smiley DL, Tashjian AH, Zhang F. Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution. J Biol Chem. 2000 Sep 1;275(35):27238-44. PMID:10837469 doi:10.1074/jbc.M001134200
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