1et3: Difference between revisions
New page: '''Theoretical Model''' The entry 1ET3 is a Theoretical Model titled 'MOLECULAR MODEL OF PTHRP (1-34) IN COMPLEX WITH THE PTH/PTHRP RECEPTOR (PTHR1).'. Category:Theoretical Model '... |
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{{Theoretical_model}} | |||
==MOLECULAR MODEL OF PTHRP (1-34) IN COMPLEX WITH THE PTH/PTHRP RECEPTOR (PTHR1).== | |||
<StructureSection load='1et3' size='340' side='right'caption='[[1et3]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
</table> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1et3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Briggs, S L]] | |||
[[Category: Chandrasekhar, S]] | |||
[[Category: Chirgadze, N Y]] | |||
[[Category: Clawson, D K]] | |||
[[Category: Jin, L]] | |||
[[Category: Schevitz, R W]] | |||
[[Category: Smiley, D L]] | |||
[[Category: Tashjian, A H]] | |||
[[Category: Zhang, F]] | |||
Latest revision as of 12:41, 21 July 2021
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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
Publication Abstract from PubMedThe 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
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