3chc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:28, 30 August 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3chc.jpg|left|200px]]
 
-
<!--
+
==Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide==
-
The line below this paragraph, containing "STRUCTURE_3chc", creates the "Structure Box" on the page.
+
<StructureSection load='3chc' size='340' side='right'caption='[[3chc]], [[Resolution|resolution]] 1.90&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'>[[3chc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHC 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]] 1.9&#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>, <scene name='pdbligand=ZRG:(2S)-2-ACETAMIDO-N-METHYL-5-[[N-(METHYLCARBAMOYL)CARBAMIMIDOYL]AMINO]PENTANAMIDE'>ZRG</scene></td></tr>
-
{{STRUCTURE_3chc| PDB=3chc | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3chc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chc OCA], [https://pdbe.org/3chc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chc RCSB], [https://www.ebi.ac.uk/pdbsum/3chc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chc ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CHIB1_ASPFM CHIB1_ASPFM] Major secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a role in the morphogenesis and autolysis (By similarity).
 +
== 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/ch/3chc_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=3chc ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Chitinase inhibitors have chemotherapeutic potential as fungicides, pesticides, and antiasthmatics. Argifin, a natural product cyclopentapeptide, competitively inhibits family 18 chitinases in the nanomolar to micromolar range and shows extensive substrate mimicry. In an attempt to map the active fragments of this large natural product, the cyclopentapeptide was progressively dissected down to four linear peptides and dimethylguanylurea, synthesized using a combination of solution and solid phase peptide synthesis. The peptide fragments inhibit chitinase B1 from Aspergillus fumigatus (AfChiB1), the human chitotriosidase, and chitinase activity in lung homogenates from a murine model of chronic asthma, with potencies ranging from high nanomolar to high micromolar inhibition. X-ray crystallographic analysis of the chitinase-inhibitor complexes revealed that the conformations of the linear peptides were remarkably similar to that of the natural product. Strikingly, the dimethylguanylurea fragment, representing only a quarter of the natural product mass, was found to harbor all significant interactions with the protein and binds with unusually high efficiency. The data provide useful information that could lead to the generation of drug-like, natural product-based chitinase inhibitors.
-
'''Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide'''
+
Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin.,Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM Chem Biol. 2008 Mar;15(3):295-301. PMID:18355729<ref>PMID:18355729</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Chitinase inhibitors have chemotherapeutic potential as fungicides, pesticides, and antiasthmatics. Argifin, a natural product cyclopentapeptide, competitively inhibits family 18 chitinases in the nanomolar to micromolar range and shows extensive substrate mimicry. In an attempt to map the active fragments of this large natural product, the cyclopentapeptide was progressively dissected down to four linear peptides and dimethylguanylurea, synthesized using a combination of solution and solid phase peptide synthesis. The peptide fragments inhibit chitinase B1 from Aspergillus fumigatus (AfChiB1), the human chitotriosidase, and chitinase activity in lung homogenates from a murine model of chronic asthma, with potencies ranging from high nanomolar to high micromolar inhibition. X-ray crystallographic analysis of the chitinase-inhibitor complexes revealed that the conformations of the linear peptides were remarkably similar to that of the natural product. Strikingly, the dimethylguanylurea fragment, representing only a quarter of the natural product mass, was found to harbor all significant interactions with the protein and binds with unusually high efficiency. The data provide useful information that could lead to the generation of drug-like, natural product-based chitinase inhibitors.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
3CHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHC OCA].
+
</div>
 +
<div class="pdbe-citations 3chc" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin., Andersen OA, Nathubhai A, Dixon MJ, Eggleston IM, van Aalten DM, Chem Biol. 2008 Mar;15(3):295-301. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18355729 18355729]
+
*[[Chitinase 3D structures|Chitinase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Aspergillus fumigatus]]
[[Category: Aspergillus fumigatus]]
-
[[Category: Chitinase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Andersen OA]]
-
[[Category: Aalten, D M.F van.]]
+
[[Category: Van Aalten DMF]]
-
[[Category: Andersen, O A.]]
+
-
[[Category: Chitinase]]
+
-
[[Category: Glycosidase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Peptide inhibitor]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:46:50 2008''
+

Current revision

Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide

PDB ID 3chc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3chc"
Personal tools