2bn2: Difference between revisions

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[[Image:2bn2.gif|left|200px]]<br /><applet load="2bn2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bn2, resolution 2.80&Aring;" />
'''CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE VASOPRESSIN ANALOGUE PHE-TYR AMIDE==
<StructureSection load='2bn2' size='340' side='right'caption='[[2bn2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bn2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bn2 1bn2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BN2 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=TYR:TYROSINE'>TYR</scene></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=2bn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bn2 OCA], [https://pdbe.org/2bn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bn2 RCSB], [https://www.ebi.ac.uk/pdbsum/2bn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bn2 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/bn/2bn2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2bn2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinated derivative. The asymmetric unit is an elongated tetramer of dimensions 110 x 40 x 30 A, composed of two dimers related by pseudo twofold symmetry. Each monomer consists of two homologous layers, each with four antiparallel beta-strands. The two regions are connected by a helix followed by a long loop. Monomer-monomer contacts involve antiparallel beta-sheet interactions, which form a dimer with two layers of eight beta-strands. One peptide per monomer occupies the principal hormone-binding pocket formed by part of the amino-terminal region and parts of the connecting helix and loop, with binding to protein consistent with conclusions drawn from solution studies. Dimer-dimer contacts involve the Tyr49 region adjacent to this site. A fifth dipeptide, of unknown biological significance, helps to stabilize one of the monomer-monomer interfaces and the tetramer-tetramer network in the crystal.
The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinated derivative. The asymmetric unit is an elongated tetramer of dimensions 110 x 40 x 30 A, composed of two dimers related by pseudo twofold symmetry. Each monomer consists of two homologous layers, each with four antiparallel beta-strands. The two regions are connected by a helix followed by a long loop. Monomer-monomer contacts involve antiparallel beta-sheet interactions, which form a dimer with two layers of eight beta-strands. One peptide per monomer occupies the principal hormone-binding pocket formed by part of the amino-terminal region and parts of the connecting helix and loop, with binding to protein consistent with conclusions drawn from solution studies. Dimer-dimer contacts involve the Tyr49 region adjacent to this site. A fifth dipeptide, of unknown biological significance, helps to stabilize one of the monomer-monomer interfaces and the tetramer-tetramer network in the crystal.


==About this Structure==
Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom.,Chen LQ, Rose JP, Breslow E, Yang D, Chang WR, Furey WF Jr, Sax M, Wang BC Proc Natl Acad Sci U S A. 1991 May 15;88(10):4240-4. PMID:2034668<ref>PMID:2034668</ref>
2BN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry 1BN2. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN2 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom., Chen LQ, Rose JP, Breslow E, Yang D, Chang WR, Furey WF Jr, Sax M, Wang BC, Proc Natl Acad Sci U S A. 1991 May 15;88(10):4240-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2034668 2034668]
</div>
<div class="pdbe-citations 2bn2" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Neurophysin|Neurophysin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Rose, J P.]]
[[Category: Rose JP]]
[[Category: Wang, B C.]]
[[Category: Wang BC]]
[[Category: complex (protein/hormone)]]
[[Category: hormone packaging]]
[[Category: transport]]
 
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