4ag1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='4ag1' size='340' side='right'caption='[[4ag1]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='4ag1' size='340' side='right'caption='[[4ag1]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4ag1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AG1 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4ag1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AG1 FirstGlance]. <br>
-
</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></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]] 1.4&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4afq|4afq]], [[1t31|1t31]], [[1klt|1klt]], [[4afs|4afs]], [[4afz|4afz]], [[1pjp|1pjp]], [[1nn6|1nn6]], [[4afu|4afu]], [[4ag2|4ag2]]</div></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></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chymase Chymase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.39 3.4.21.39] </span></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=4ag1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag1 OCA], [https://pdbe.org/4ag1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ag1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ag1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ag1 ProSAT]</span></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=4ag1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag1 OCA], [https://pdbe.org/4ag1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ag1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ag1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ag1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/CMA1_HUMAN CMA1_HUMAN]] Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
+
[https://www.uniprot.org/uniprot/CMA1_HUMAN CMA1_HUMAN] Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The serine protease chymase (EC = 3.4.21.39) is expressed in the secretory granules of mast cells, which are important in allergic reactions. Fynomers, which are binding proteins derived from the Fyn SH3 domain, were generated against human chymase to produce binding partners to facilitate crystallization, structure determination and structure-based drug discovery, and to provide inhibitors of chymase for therapeutic applications. The best Fynomer was found to bind chymase with a KD of 0.9 nM and koff of 6.6x10 (-4) s (-1) , and to selectively inhibit chymase activity with an IC 50 value of 2 nM. Three different Fynomers were co-crystallized with chymase in 6 different crystal forms overall, with diffraction quality in the range of 2.25 to 1.4 A resolution, which is suitable for drug design efforts. The X-ray structures show that all Fynomers bind to the active site of chymase. The conserved residues Arg15-Trp16-Thr17 in the RT-loop of the chymase binding Fynomers provide a tight interaction, with Trp16 pointing deep into the S1 pocket of chymase. These results confirm the suitability of Fynomers as research tools to facilitate protein crystallization, as well as for the development of assays to investigate the biological mechanism of targets. Finally, their highly specific inhibitory activity and favorable molecular properties support the use of Fynomers as potential therapeutic agents.
+
-
 
+
-
Generation, characterization and structural data of chymase binding proteins based on the human Fyn kinase SH3 domain.,Schlatter D, Brack S, Banner DW, Batey S, Benz J, Bertschinger J, Huber W, Joseph C, Rufer A, van der Klooster A, Weber M, Grabulovski D, Hennig M MAbs. 2012 Jul 1;4(4):497-508. Epub 2012 Jul 1. PMID:22653218<ref>PMID:22653218</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4ag1" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Chymase]]
+
[[Category: Homo sapiens]]
-
[[Category: Human]]
+
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Synthetic construct sequences]]
+
[[Category: Synthetic construct]]
-
[[Category: Banner, D W]]
+
[[Category: Banner DW]]
-
[[Category: Batey, S]]
+
[[Category: Batey S]]
-
[[Category: Benz, J]]
+
[[Category: Benz J]]
-
[[Category: Bertschinger, J]]
+
[[Category: Bertschinger J]]
-
[[Category: Brack, S]]
+
[[Category: Brack S]]
-
[[Category: Grabulovski, D]]
+
[[Category: Grabulovski D]]
-
[[Category: Hennig, M]]
+
[[Category: Hennig M]]
-
[[Category: Huber, W]]
+
[[Category: Huber W]]
-
[[Category: Joseph, C]]
+
[[Category: Joseph C]]
-
[[Category: Kloosters, A Van Der]]
+
[[Category: Rufer A]]
-
[[Category: Rufer, A]]
+
[[Category: Schlatter D]]
-
[[Category: Schlatter, D]]
+
[[Category: Van Der Kloosters A]]
-
[[Category: Weber, M]]
+
[[Category: Weber M]]
-
[[Category: Hydrolase-de novo protein complex]]
+
-
[[Category: Inhibitor]]
+
-
[[Category: Serine protease]]
+

Revision as of 07:14, 1 May 2024

Human Chymase - Fynomer Complex

PDB ID 4ag1

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/4ag1"
Personal tools