This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2b19

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 13:04, 24 November 2021

Solution Structure of mammalian tachykinin peptide, Neuropeptide K

Structural highlights

2b19 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TKN1_HUMAN] Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.

Publication Abstract from PubMed

Neuropeptide K (NPK), an N-terminally extended form of neurokinin A (NKA), represents the most potent and longest lasting vasodepressor and cardiomodulatory tachykinin reported thus far. NPK has been shown to have high selectivity for the NK2 receptor. Because the micelle-associated structure may be relevant to the NPK-receptor interaction, the three-dimensional structure of the NPK in aqueous and micellar environments has been studied by two-dimensional proton nuclear magnetic resonance (2D (1)H NMR spectroscopy) and distance geometry calculations. Proton NMR assignments have been carried out with the aid of correlation spectroscopy (DQF-COSY and TOCSY) and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The interproton distances and dihedral angle constraints obtained from the NMR data have been used in torsion angle dynamics algorithm for NMR applications (DYANA) to generate a family of structures, which have been refined using restrained energy minimization and dynamics. The results show that in an aqueous environment NPK lacks a definite secondary structure, although some turn-like elements are present in the N terminus. The structure is well-defined in the presence of dodecylphosphocholine micelles. The global fold of NPK bound to DPC micelles consists of two well-defined helices from residues 9 to 18 and residues 27 to 33 connected by a noncanonical beta turn. The N terminus of the peptide is characterized by a 3(10) helix or a series of dynamic beta turns. The conformational range of the peptide revealed by NMR and circular dichroism (CD) studies has been analyzed in terms of characteristic secondary features. The observed conformational features have been further compared to a NKA and neuropeptide gamma (NPgamma) potent endogenous agonist for the NK2 receptor.

Three-dimensional structure of neuropeptide k bound to dodecylphosphocholine micelles.,Dike A, Cowsik SM Biochemistry. 2006 Mar 7;45(9):2994-3004. PMID:16503654^[1]

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

References

↑ Dike A, Cowsik SM. Three-dimensional structure of neuropeptide k bound to dodecylphosphocholine micelles. Biochemistry. 2006 Mar 7;45(9):2994-3004. PMID:16503654 doi:10.1021/bi052287o

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b19"

@@ Line 3: / Line 3: @@
 <StructureSection load='2b19' size='340' side='right'caption='[[2b19]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2b19]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B19 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2b19]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B19 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b19 OCA], [http://pdbe.org/2b19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b19 RCSB], [http://www.ebi.ac.uk/pdbsum/2b19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b19 ProSAT]</span></td></tr>
+</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=2b19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b19 OCA], [https://pdbe.org/2b19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b19 RCSB], [https://www.ebi.ac.uk/pdbsum/2b19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b19 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TKN1_HUMAN TKN1_HUMAN]] Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.
+[[https://www.uniprot.org/uniprot/TKN1_HUMAN TKN1_HUMAN]] Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2b19

From Proteopedia

Revision as of 13:04, 24 November 2021

Solution Structure of mammalian tachykinin peptide, Neuropeptide K

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox