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.


1tz4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1tz4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tz4" /> '''[hPP19-23]-pNPY bound to DPC Micelles'''<br ...)
Current revision (08:45, 1 May 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1tz4.gif|left|200px]]<br /><applet load="1tz4" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1tz4" />
 
-
'''[hPP19-23]-pNPY bound to DPC Micelles'''<br />
 
-
==Overview==
+
==[hPP19-23]-pNPY bound to DPC Micelles==
-
Neuropeptide Y (NPY) and the pancreatic polypeptide (PP) are members of, the neuropeptide Y family of hormones. They bind to the Y receptors with, very different affinities: Whereas PP is highly selective for the Y(4), receptor, NPY displays highest affinites for Y(1), Y(2), and Y(5) receptor, subtypes. Introducing the NPY segment 19-23 into PP leads to an increase, in affinity at the Y(1) and Y(2) receptor subtypes whereas the exchange of, this segment from PP into NPY leads to a large decrease in affinity at all, receptor subtypes. PP displays a very stable structure in solution, with, the N terminus being back-folded onto the C-terminal alpha-helix (the, so-called PP-fold). The helix of NPY is less stable and the N terminus is, freely diffusing in solution. The exchange of this segment, however, does, not alter the PP-fold propensities of the chimeric peptides in solution., The structures of the phospholipid micelle-bound peptides serving to mimic, the membrane-bound species display segregation into a more flexible, N-terminal region and a well-defined alpha-helical region. The, introduction of the [19-23]-pNPY segment into hPP leads to an N-terminal, extension of the alpha-helix, now starting at Pro(14) instead of Met(17)., In contrast, a truncated helix is observed in [(19)(-)(23)hPP]-pNPY, starting at Leu(17) instead of Ala(14). All peptides display moderate, binding affinities to neutral membranes (K(assoc) in the range of 1.7 to, 6.8 x 10(4) mol(-)(1) as determined by surface plasmon resonance) with the, differences in binding being most probably related to the exchange of, Arg-19 (pNPY) by Glu-23 (hPP). Differences in receptor binding properties, between the chimeras and their parental peptides are therefore most likely, due to changes in the conformation of the micelle-bound peptides.
+
<StructureSection load='1tz4' size='340' side='right'caption='[[1tz4]]' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1tz4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TZ4 FirstGlance]. <br>
-
1TZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa_and_homo_sapiens Sus scrofa and homo sapiens] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TZ4 OCA].
+
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tz4 OCA], [https://pdbe.org/1tz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tz4 RCSB], [https://www.ebi.ac.uk/pdbsum/1tz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tz4 ProSAT]</span></td></tr>
-
Strongly altered receptor binding properties in PP and NPY chimeras are accompanied by changes in structure and membrane binding., Lerch M, Kamimori H, Folkers G, Aguilar MI, Beck-Sickinger AG, Zerbe O, Biochemistry. 2005 Jun 28;44(25):9255-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15966750 15966750]
+
</table>
-
[[Category: Single protein]]
+
== Function ==
-
[[Category: Sus scrofa and homo sapiens]]
+
[https://www.uniprot.org/uniprot/NPY_PIG NPY_PIG] NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.[https://www.uniprot.org/uniprot/PAHO_HUMAN PAHO_HUMAN] Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions. The physiological role for the icosapeptide has not yet been elucidated.
-
[[Category: Aguilar, M.I.]]
+
== Evolutionary Conservation ==
-
[[Category: Beck-Sickinger, A.G.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Folkers, G.]]
+
Check<jmol>
-
[[Category: Kamimori, H.]]
+
<jmolCheckbox>
-
[[Category: Lerch, M.]]
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tz/1tz4_consurf.spt"</scriptWhenChecked>
-
[[Category: Zerbe, O.]]
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
[[Category: NH2]]
+
<text>to colour the structure by Evolutionary Conservation</text>
-
[[Category: npy-pp chimera]]
+
</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=1tz4 ConSurf].
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:42:48 2007''
+
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Sus scrofa]]
 +
[[Category: Aguilar MI]]
 +
[[Category: Beck-Sickinger AG]]
 +
[[Category: Folkers G]]
 +
[[Category: Kamimori H]]
 +
[[Category: Lerch M]]
 +
[[Category: Zerbe O]]

Current revision

[hPP19-23]-pNPY bound to DPC Micelles

PDB ID 1tz4

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/1tz4"
Personal tools