3lpp: Difference between revisions

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==Crystal complex of N-terminal sucrase-isomaltase with kotalanol==
==Crystal complex of N-terminal sucrase-isomaltase with kotalanol==
<StructureSection load='3lpp' size='340' side='right' caption='[[3lpp]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3lpp' size='340' side='right'caption='[[3lpp]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3lpp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LPP FirstGlance]. <br>
<table><tr><td colspan='2'>[[3lpp]] is a 4 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=3LPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LPP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KTL:(1S,2R,3R,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-DIHYDROXY-2-(HYDROXYMETHYL)TETRAHYDROTHIOPHENIUM-1-YL]-1-HYDROXYETHYL}-2,3,4,5-TETRAHYDROXYPENTYL+SULFATE'>KTL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lpo|3lpo]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KTL:(1S,2R,3R,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-DIHYDROXY-2-(HYDROXYMETHYL)TETRAHYDROTHIOPHENIUM-1-YL]-1-HYDROXYETHYL}-2,3,4,5-TETRAHYDROXYPENTYL+SULFATE'>KTL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3lpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lpp OCA], [https://pdbe.org/3lpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lpp RCSB], [https://www.ebi.ac.uk/pdbsum/3lpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lpp ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oligo-1,6-glucosidase Oligo-1,6-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.10 3.2.1.10] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lpp OCA], [http://pdbe.org/3lpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lpp RCSB], [http://www.ebi.ac.uk/pdbsum/3lpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lpp ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/SUIS_HUMAN SUIS_HUMAN]] Congenital sucrase-isomaltase deficiency. Defects in SI are the cause of congenital sucrase-isomaltase deficiency (CSID) [MIM:[http://omim.org/entry/222900 222900]]; also known as disaccharide intolerance I. CSID is an autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI.<ref>PMID:8609217</ref> <ref>PMID:10903344</ref> <ref>PMID:11340066</ref> <ref>PMID:14724820</ref> <ref>PMID:16329100</ref>
[https://www.uniprot.org/uniprot/SUIS_HUMAN SUIS_HUMAN] Congenital sucrase-isomaltase deficiency. Defects in SI are the cause of congenital sucrase-isomaltase deficiency (CSID) [MIM:[https://omim.org/entry/222900 222900]; also known as disaccharide intolerance I. CSID is an autosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI.<ref>PMID:8609217</ref> <ref>PMID:10903344</ref> <ref>PMID:11340066</ref> <ref>PMID:14724820</ref> <ref>PMID:16329100</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SUIS_HUMAN SUIS_HUMAN]] Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.<ref>PMID:20356844</ref>
[https://www.uniprot.org/uniprot/SUIS_HUMAN SUIS_HUMAN] Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.<ref>PMID:20356844</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/3lpp_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/3lpp_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 3lpp" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3lpp" style="background-color:#fffaf0;"></div>
==See Also==
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Oligo-1,6-glucosidase]]
[[Category: Large Structures]]
[[Category: Rose, D R]]
[[Category: Rose DR]]
[[Category: Sim, L]]
[[Category: Sim L]]
[[Category: Alpha-glucosidase]]
[[Category: Cell membrane]]
[[Category: Disease mutation]]
[[Category: Disulfide bond]]
[[Category: Glycoprotein]]
[[Category: Glycosidase]]
[[Category: Glycoside hydrolase family 31]]
[[Category: Hydrolase]]
[[Category: Isomaltase]]
[[Category: Membrane]]
[[Category: Multifunctional enzyme]]
[[Category: Polymorphism]]
[[Category: Signal-anchor]]
[[Category: Sulfation]]
[[Category: Transmembrane]]

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