1fn0: Difference between revisions

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-{{Seed}}
-[[Image:1fn0.png|left|200px]]
-<!--
+==STRUCTURE OF A MUTANT WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN, N14D.==
-The line below this paragraph, containing "STRUCTURE_1fn0", creates the "Structure Box" on the page.
+<StructureSection load='1fn0' size='340' side='right'caption='[[1fn0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1fn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FN0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_1fn0|  PDB=1fn0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fn0 OCA], [https://pdbe.org/1fn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fn0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ICW3_PSOTE ICW3_PSOTE] Inhibits alpha-chymotrypsin at the molar ratio of 1:2 in state of 1:1.
+== 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/fn/1fn0_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=1fn0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A double-headed chymotrypsin inhibitor, WCI, from winged bean seeds was cloned for structural and biochemical studies. The inhibitor was subjected to two point mutations at a conserved position, Asn14. This residue, known to have a pivotal role in stabilizing the first reactive-site loop (Gln63-Phe68) of the inhibitor, is highly conserved in the sequences of the other members of Kunitz (STI) family as well as in the sequences of Kazal family of serine protease inhibitors. The mutants, N14K and N14D, were subjected to biochemical assay and their characteristics were compared with those of the recombinant inhibitor (rWCI). Crystallographic studies of the recombinant and the mutant proteins are discussed. These studies were primarily aimed at understanding the importance of the protein scaffolding towards the conformational rigidity of the reactive-site loop. Our analysis reveals that, as the Lys14 side chain takes an unusual fold in N14K and the Asp14 side chain in N14D interacts with the loop residues by water-mediated hydrogen bonds, the canonical conformation of the loop has remained effectively intact in both the mutant structures. However, minor alterations such as a 2-fold increase in the inhibitory affinity towards the cognate enzyme were observed.
-===STRUCTURE OF A MUTANT WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN, N14D.===
+The role of Asn14 in the stability and conformation of the reactive-site loop of winged bean chymotrypsin inhibitor: crystal structures of two point mutants Asn14--&gt;Lys and Asn14--&gt;Asp.,Ravichandran S, Dasgupta J, Chakrabarti C, Ghosh S, Singh M, Dattagupta JK Protein Eng. 2001 May;14(5):349-57. PMID:11438758<ref>PMID:11438758</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1fn0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11438758}}, adds the Publication Abstract to the page
+*[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11438758 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11438758}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-FN0 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FN0 OCA].
-==Reference==
-<ref group="xtra">PMID:11438758</ref><references group="xtra"/>
 [[Category: Psophocarpus tetragonolobus]]
-[[Category: Chakrabarti, C.]]
+[[Category: Chakrabarti C]]
-[[Category: Dasgupta, J.]]
+[[Category: Dasgupta J]]
-[[Category: Dattagupta, J K.]]
+[[Category: Dattagupta JK]]
-[[Category: Ghosh, S.]]
+[[Category: Ghosh S]]
-[[Category: Ravichandran, S.]]
+[[Category: Ravichandran S]]
-[[Category: Beta trefoil]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:16:18 2009''