1hki

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:17, 9 October 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hki.jpg|left|200px]]
 
-
{{Structure
+
==Crystal structure of human chitinase in complex with glucoallosamidin B==
-
|PDB= 1hki |SIZE=350|CAPTION= <scene name='initialview01'>1hki</scene>, resolution 2.55&Aring;
+
<StructureSection load='1hki' size='340' side='right'caption='[[1hki]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=AC1:Ali+Binding+Site+For+Chain+A'>AC1</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NA1:METHYL+N-ACETYL+ALLOSAMINE'>NA1</scene> and <scene name='pdbligand=ALI:METHYL N-ACETYL ALLOSAMINE'>ALI</scene>
+
<table><tr><td colspan='2'>[[1hki]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HKI FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALI:METHYL+N-ACETYL+ALLOSAMINE'>ALI</scene>, <scene name='pdbligand=NA1:METHYL+N-ACETYL+ALLOSAMINE'>NA1</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1hki FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hki OCA], [https://pdbe.org/1hki PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hki RCSB], [https://www.ebi.ac.uk/pdbsum/1hki PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hki ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CHIT1_HUMAN CHIT1_HUMAN] Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity.<ref>PMID:7592832</ref> <ref>PMID:7836450</ref> <ref>PMID:9748235</ref>
 +
== 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/hk/1hki_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=1hki ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The pseudotrisaccharide allosamidin is a potent family 18 chitinase inhibitor with demonstrated biological activity against insects, fungi, and the Plasmodium falciparum life cycle. The synthesis and biological properties of several derivatives have been reported. The structural interactions of allosamidin with several family 18 chitinases have been determined by x-ray crystallography previously. Here, a high resolution structure of chitotriosidase, the human macrophage chitinase, in complex with allosamidin is presented. In addition, complexes of the allosamidin derivatives demethylallosamidin, methylallosamidin, and glucoallosamidin B are described, together with their inhibitory properties. Similar to other chitinases, inhibition of the human chitinase by allosamidin derivatives lacking a methyl group is 10-fold stronger, and smaller effects are observed for the methyl and C3 epimer derivatives. The structures explain the effects on inhibition in terms of altered hydrogen bonding and hydrophobic interactions, together with displaced water molecules. The data reported here represent a first step toward structure-based design of specific allosamidin derivatives.
-
'''CRYSTAL STRUCTURE OF HUMAN CHITINASE IN COMPLEX WITH GLUCOALLOSAMIDIN B'''
+
Crystal structures of allosamidin derivatives in complex with human macrophage chitinase.,Rao FV, Houston DR, Boot RG, Aerts JM, Sakuda S, van Aalten DM J Biol Chem. 2003 May 30;278(22):20110-6. Epub 2003 Mar 14. PMID:12639956<ref>PMID:12639956</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1hki" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The pseudotrisaccharide allosamidin is a potent family 18 chitinase inhibitor with demonstrated biological activity against insects, fungi, and the Plasmodium falciparum life cycle. The synthesis and biological properties of several derivatives have been reported. The structural interactions of allosamidin with several family 18 chitinases have been determined by x-ray crystallography previously. Here, a high resolution structure of chitotriosidase, the human macrophage chitinase, in complex with allosamidin is presented. In addition, complexes of the allosamidin derivatives demethylallosamidin, methylallosamidin, and glucoallosamidin B are described, together with their inhibitory properties. Similar to other chitinases, inhibition of the human chitinase by allosamidin derivatives lacking a methyl group is 10-fold stronger, and smaller effects are observed for the methyl and C3 epimer derivatives. The structures explain the effects on inhibition in terms of altered hydrogen bonding and hydrophobic interactions, together with displaced water molecules. The data reported here represent a first step toward structure-based design of specific allosamidin derivatives.
+
*[[Chitinase 3D structures|Chitinase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1HKI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKI OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Crystal structures of allosamidin derivatives in complex with human macrophage chitinase., Rao FV, Houston DR, Boot RG, Aerts JM, Sakuda S, van Aalten DM, J Biol Chem. 2003 May 30;278(22):20110-6. Epub 2003 Mar 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12639956 12639956]
+
-
[[Category: Chitinase]]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Aalten, D M.F Van.]]
+
[[Category: Aerts JMFG]]
-
[[Category: Aerts, J M.F G.]]
+
[[Category: Boot RG]]
-
[[Category: Boot, R G.]]
+
[[Category: Houston DR]]
-
[[Category: Houston, D R.]]
+
[[Category: Rao FV]]
-
[[Category: Rao, F V.]]
+
[[Category: Sakuda S]]
-
[[Category: Sakuda, S.]]
+
[[Category: Van Aalten DMF]]
-
[[Category: ALI]]
+
-
[[Category: NA1]]
+
-
[[Category: NAG]]
+
-
[[Category: allosamidin]]
+
-
[[Category: glucoallosamidin b]]
+
-
[[Category: human chitinase]]
+
-
[[Category: hydrolase]]
+
-
[[Category: structure]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:19 2008''
+

Current revision

Crystal structure of human chitinase in complex with glucoallosamidin B

PDB ID 1hki

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/1hki"
Personal tools