2bua: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image: | ==CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A LOW MOLECULAR WEIGHT INHIBITOR.== | ||
<StructureSection load='2bua' size='340' side='right' caption='[[2bua]], [[Resolution|resolution]] 2.56Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bua]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BUA FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=007:1-METHYLAMINE-1-BENZYL-CYCLOPENTANE'>007</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1orv|1orv]], [[1orw|1orw]], [[2buc|2buc]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bua OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bua RCSB], [http://www.ebi.ac.uk/pdbsum/2bua PDBsum]</span></td></tr> | |||
<table> | |||
== 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/bu/2bua_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The co-crystal structure of beta-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. This finding provided the basis for a general hypothesis of a reverse binding mode for beta-phenethylamine-based DPP-IV inhibitors. Novel inhibitor design concepts that obviate substrate-like structure-activity relationships (SAR) were thereby enabled, and novel, potent inhibitors were discovered. | |||
The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors.,Nordhoff S, Cerezo-Galvez S, Feurer A, Hill O, Matassa VG, Metz G, Rummey C, Thiemann M, Edwards PJ Bioorg Med Chem Lett. 2006 Mar 15;16(6):1744-8. Epub 2006 Jan 11. PMID:16376544<ref>PMID:16376544</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Dipeptidyl peptidase|Dipeptidyl peptidase]] | *[[Dipeptidyl peptidase|Dipeptidyl peptidase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Dipeptidyl-peptidase IV]] | [[Category: Dipeptidyl-peptidase IV]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
Revision as of 07:23, 29 September 2014
CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A LOW MOLECULAR WEIGHT INHIBITOR.CRYSTAL STRUCTURE OF PORCINE DIPEPTIDYL PEPTIDASE IV (CD26) IN COMPLEX WITH A LOW MOLECULAR WEIGHT INHIBITOR.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe co-crystal structure of beta-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. This finding provided the basis for a general hypothesis of a reverse binding mode for beta-phenethylamine-based DPP-IV inhibitors. Novel inhibitor design concepts that obviate substrate-like structure-activity relationships (SAR) were thereby enabled, and novel, potent inhibitors were discovered. The reversed binding of beta-phenethylamine inhibitors of DPP-IV: X-ray structures and properties of novel fragment and elaborated inhibitors.,Nordhoff S, Cerezo-Galvez S, Feurer A, Hill O, Matassa VG, Metz G, Rummey C, Thiemann M, Edwards PJ Bioorg Med Chem Lett. 2006 Mar 15;16(6):1744-8. Epub 2006 Jan 11. PMID:16376544[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Dipeptidyl-peptidase IV
- Sus scrofa
- Cerezo-Galvez, S.
- Edwards, P J.
- Feurer, A.
- Hill, O.
- Matassa, V G.
- Metz, G.
- Nordhoff, S.
- Rummey, C.
- Thiemann, M.
- Aminopeptidase
- Diabetes mellitus
- Dpp-iv
- Drug design
- Glycoprotein
- Hydrolase
- Hydrolase-inhibitor complex
- Hydrolase/inhibitor
- Protease
- Serine protease
- Signal- anchor
- Transmembrane