View source for 1npo


==BOVINE NEUROPHYSIN II COMPLEX WITH OXYTOCIN==
<StructureSection load='1npo' size='340' side='right'caption='[[1npo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1npo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NPO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=1npo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npo OCA], [https://pdbe.org/1npo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1npo RCSB], [https://www.ebi.ac.uk/pdbsum/1npo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1npo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NEU2_BOVIN NEU2_BOVIN] Neurophysin 2 specifically binds vasopressin.  Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/np/1npo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=1npo ConSurf].
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== Publication Abstract from PubMed ==
The first crystal structure of the pituitary hormone oxytocin complexed with its carrier protein neurophysin has been determined and refined to 3.0 A resolution. The hormone-binding site is located at the end of a 3(10)-helix and involves residues from both domains of each monomer. Hormone residues Tyr 2, which is buried deep in the binding pocket, and Cys 1 have been confirmed as the key residues involved in neurophysin-hormone recognition. We have compared the bound oxytocin observed in the neurophysin-oxytocin complex, the X-ray structures of unbound oxytocin analogues and the NMR-derived structure for bound oxytocin. We find that while our structure is in agreement with the previous crystallographic findings, it differs from the NMR result with regard to how Tyr 2 of the hormone is recognized by neurophysin.

Crystal structure of the neurophysin-oxytocin complex.,Rose JP, Wu CK, Hsiao CD, Breslow E, Wang BC Nat Struct Biol. 1996 Feb;3(2):163-9. PMID:8564543<ref>PMID:8564543</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1npo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Neurophysin|Neurophysin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Rose JP]]
[[Category: Wang B-C]]