2n2f

From Proteopedia

(Difference between revisions)

Current revision

Solution NMR structure of Dynorphin 1-13 bound to Kappa Opioid Receptor

Structural highlights

2n2f is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PDYN_HUMAN Spinocerebellar ataxia type 23. The disease is caused by mutations affecting the gene represented in this entry.

Function

PDYN_HUMAN Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity). Leumorphin has a typical opiod activity and may have anti-apoptotic effect.

Publication Abstract from PubMed

The structure of the dynorphin (1-13) peptide (dynorphin) bound to the human kappa opioid receptor (KOR) has been determined by liquid-state NMR spectroscopy. (1)H and (15)N chemical shift variations indicated that free and bound peptide is in fast exchange in solutions containing 1 mM dynorphin and 0.01 mM KOR. Radioligand binding indicated an intermediate-affinity interaction, with a Kd of approximately 200 nM. Transferred nuclear Overhauser enhancement spectroscopy was used to determine the structure of bound dynorphin. The N-terminal opioid signature, YGGF, was observed to be flexibly disordered, the central part of the peptide from L5 to R9 to form a helical turn, and the C-terminal segment from P10 to K13 to be flexibly disordered in this intermediate-affinity bound state. Combining molecular modeling with NMR provided an initial framework for understanding multistep activation of a G protein-coupled receptor by its cognate peptide ligand.

NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor.,O'Connor C, White KL, Doncescu N, Didenko T, Roth BL, Czaplicki G, Stevens RC, Wuthrich K, Milon A Proc Natl Acad Sci U S A. 2015 Sep 22;112(38):11852-7. doi:, 10.1073/pnas.1510117112. Epub 2015 Sep 8. PMID:26372966^[1]

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

References

↑ O'Connor C, White KL, Doncescu N, Didenko T, Roth BL, Czaplicki G, Stevens RC, Wuthrich K, Milon A. NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor. Proc Natl Acad Sci U S A. 2015 Sep 22;112(38):11852-7. doi:, 10.1073/pnas.1510117112. Epub 2015 Sep 8. PMID:26372966 doi:http://dx.doi.org/10.1073/pnas.1510117112

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2n2f"

@@ Line 1: / Line 1: @@
 ==Solution NMR structure of Dynorphin 1-13 bound to Kappa Opioid Receptor==
-<StructureSection load='2n2f' size='340' side='right'caption='[[2n2f]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2n2f' size='340' side='right'caption='[[2n2f]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2n2f]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N2F FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2n2f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N2F 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=2n2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n2f OCA], [https://pdbe.org/2n2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n2f RCSB], [https://www.ebi.ac.uk/pdbsum/2n2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n2f ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2n2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n2f OCA], [https://pdbe.org/2n2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n2f RCSB], [https://www.ebi.ac.uk/pdbsum/2n2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n2f ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/PDYN_HUMAN PDYN_HUMAN]] Spinocerebellar ataxia type 23. The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/PDYN_HUMAN PDYN_HUMAN] Spinocerebellar ataxia type 23. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[https://www.uniprot.org/uniprot/PDYN_HUMAN PDYN_HUMAN]] Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity).  Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity).  Leumorphin has a typical opiod activity and may have anti-apoptotic effect.
+[https://www.uniprot.org/uniprot/PDYN_HUMAN PDYN_HUMAN] Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity).  Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700 times more potent than Leu-enkephalin (By similarity).  Leumorphin has a typical opiod activity and may have anti-apoptotic effect.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Connor, C O]]
+[[Category: Czaplicki G]]
-[[Category: Czaplicki, G]]
+[[Category: Didenko T]]
-[[Category: Didenko, T]]
+[[Category: Doncescu N]]
-[[Category: Doncescu, N]]
+[[Category: Milon A]]
-[[Category: Milon, A]]
+[[Category: O'Connor C]]
-[[Category: Roth, B L]]
+[[Category: Roth BL]]
-[[Category: Stevens, R C]]
+[[Category: Stevens RC]]
-[[Category: White, K]]
+[[Category: White K]]
-[[Category: Wuthrich, K]]
+[[Category: Wuthrich K]]
-[[Category: Gpcr]]
-[[Category: Hormone receptor]]

2n2f

From Proteopedia

Current revision

Solution NMR structure of Dynorphin 1-13 bound to Kappa Opioid Receptor

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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