1yf4: Difference between revisions

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[[Image:1yf4.gif|left|200px]]
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{{STRUCTURE_1yf4|  PDB=1yf4  |  SCENE=  }}
'''Crystal Structure of trypsin-vasopressin complex'''


==Crystal Structure of trypsin-vasopressin complex==
<StructureSection load='1yf4' size='340' side='right'caption='[[1yf4]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yf4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YF4 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]] 1.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1yf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yf4 OCA], [https://pdbe.org/1yf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yf4 RCSB], [https://www.ebi.ac.uk/pdbsum/1yf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yf4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRYP_PIG TRYP_PIG]
== 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/yf/1yf4_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=1yf4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The large variety of serine protease inhibitors, available from various sources such as tissues, microorganisms, plants, etc., play an important role in regulating the proteolytic enzymes. The analysis of protease-inhibitor complexes helps in understanding the mechanism of action, as well as in designing inhibitors. Vasopressin, an anti-diuretic nonapeptide hormone, is found to be an effective inhibitor of trypsin, with a K(i) value of 5 nM. The crystal structure of the trypsin-vasopressin complex revealed that vasopressin fulfils all the important interactions for an inhibitor, without any break in the scissile peptide bond. The cyclic nature due to a disulfide bridge between Cys1 and Cys6 of vasopressin provides structural rigidity to the peptide hormone. The trypsin-binding site is located at the C terminus, while the neurophysin-binding site is at the N terminus of vasopressin. This study will assist in designing new peptide inhibitors. This study suggests that vasopressin inhibition of trypsin may have unexplored biological implications.


==Overview==
Trypsin inhibition by a peptide hormone: crystal structure of trypsin-vasopressin complex.,Syed Ibrahim B, Pattabhi V J Mol Biol. 2005 May 20;348(5):1191-8. Epub 2005 Apr 1. PMID:15854654<ref>PMID:15854654</ref>
The large variety of serine protease inhibitors, available from various sources such as tissues, microorganisms, plants, etc., play an important role in regulating the proteolytic enzymes. The analysis of protease-inhibitor complexes helps in understanding the mechanism of action, as well as in designing inhibitors. Vasopressin, an anti-diuretic nonapeptide hormone, is found to be an effective inhibitor of trypsin, with a K(i) value of 5 nM. The crystal structure of the trypsin-vasopressin complex revealed that vasopressin fulfils all the important interactions for an inhibitor, without any break in the scissile peptide bond. The cyclic nature due to a disulfide bridge between Cys1 and Cys6 of vasopressin provides structural rigidity to the peptide hormone. The trypsin-binding site is located at the C terminus, while the neurophysin-binding site is at the N terminus of vasopressin. This study will assist in designing new peptide inhibitors. This study suggests that vasopressin inhibition of trypsin may have unexplored biological implications.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1YF4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YF4 OCA].
</div>
<div class="pdbe-citations 1yf4" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Trypsin inhibition by a peptide hormone: crystal structure of trypsin-vasopressin complex., Syed Ibrahim B, Pattabhi V, J Mol Biol. 2005 May 20;348(5):1191-8. Epub 2005 Apr 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15854654 15854654]
*[[Trypsin 3D structures|Trypsin 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Trypsin]]
[[Category: Pattabhi V]]
[[Category: Ibrahim, B Syed.]]
[[Category: Syed Ibrahim B]]
[[Category: Pattabhi, V.]]
[[Category: Peptide binding]]
[[Category: Trypsin]]
[[Category: Vasopressin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:14:39 2008''
Retrieved from "https://proteopedia.org/1yf4"