View source for 1ccv


==NMR SOLUTION STRUCTURE OF APIS MELLIFERA CHYMOTRYPSIN INHIBITOR (AMCI).==
<StructureSection load='1ccv' size='340' side='right'caption='[[1ccv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ccv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1ccv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ccv OCA], [https://pdbe.org/1ccv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ccv RCSB], [https://www.ebi.ac.uk/pdbsum/1ccv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ccv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMCI_APIME AMCI_APIME] 
== 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/cc/1ccv_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=1ccv ConSurf].
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== Publication Abstract from PubMed ==
The three-dimensional structure of the 56 residue polypeptide Apis mellifera chymotrypsin/cathepsin G inhibitor 1 (AMCI-1) isolated from honey bee hemolymph was calculated based on 730 experimental NMR restraints. It consists of two approximately perpendicular beta-sheets, several turns, and a long exposed loop that includes the protease binding site. The lack of extensive secondary structure features or hydrophobic core is compensated by the presence of five disulfide bridges that stabilize both the protein scaffold and the binding loop segment. A detailed analysis of the protease binding loop conformation reveals that it is similar to those found in other canonical serine protease inhibitors. The AMCI-1 structure exhibits a common fold with a novel family of inhibitors from the intestinal parasitic worm Ascaris suum. The pH-induced conformational changes in the binding loop region observed in the Ascaris inhibitor ATI are absent in AMCI-1. Similar binding site sequences and structures strongly suggest that the lack of the conformational change can be attributed to a Glu--&gt;Gln substitution at the P1' position in AMCI-1, compared to ATI. Analysis of amide proton temperature coefficients shows very good correlation with the presence of hydrogen bond donors in the calculated AMCI-1 structure.

NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.,Cierpicki T, Bania J, Otlewski J Protein Sci. 2000 May;9(5):976-84. PMID:10850807<ref>PMID:10850807</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 1ccv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Apis mellifera]]
[[Category: Large Structures]]
[[Category: Cierpicki T]]
[[Category: Otlewski J]]