This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2f9o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:23, 30 August 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2f9o.png|left|200px]]
 
-
<!--
+
==Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G==
-
The line below this paragraph, containing "STRUCTURE_2f9o", creates the "Structure Box" on the page.
+
<StructureSection load='2f9o' size='340' side='right'caption='[[2f9o]], [[Resolution|resolution]] 2.10&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'>[[2f9o]] 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=2F9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F9O 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]] 2.1&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-
{{STRUCTURE_2f9o| PDB=2f9o | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9o OCA], [https://pdbe.org/2f9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f9o RCSB], [https://www.ebi.ac.uk/pdbsum/2f9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9o ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRYB1_HUMAN TRYB1_HUMAN] Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type (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/f9/2f9o_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=2f9o ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Tryptases alpha and beta are trypsin-like serine proteinases expressed in large amounts by mast cells. Beta-tryptase is a tetramer that has enzymatic activity, but requires heparin binding to maintain functional and structural stability, whereas alpha-tryptase has little, if any, enzymatic activity but is a stable tetramer in the absence of heparin. As shown previously, these differences can be mainly attributed to the different conformations of the 214-220 segment. Interestingly, the replacement of Asp216 by Gly, which is present in beta-tryptase, results in enzymatically active but less stable alpha-tryptase mutants. We have solved the crystal structures of both the single (D216G) and the double (K192Q/D216G) mutant forms of recombinant human alphaI-tryptase in complex with the peptide inhibitor leupeptin, as well as the structure of the non-inhibited single mutant. The inhibited mutants exhibited an open functional substrate binding site, while in the absence of an inhibitor, the open (beta-tryptase-like) and the closed (alpha-tryptase-like) conformations were present simultaneously. This shows that both forms are in a two-state equilibrium, which is influenced by the residues in the vicinity of the active site and by inhibitor/substrate binding. Novel insights regarding the observed stability differences as well as a potential proteolytic activity of wild-type alpha-tryptase, which may possess a cryptic active site, are discussed.
-
===Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G===
+
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha--&gt;beta-tryptase transition.,Rohr KB, Selwood T, Marquardt U, Huber R, Schechter NM, Bode W, Than ME J Mol Biol. 2006 Mar 17;357(1):195-209. Epub 2005 Dec 28. PMID:16414069<ref>PMID:16414069</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2f9o" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_16414069}}, adds the Publication Abstract to the page
+
*[[Tryptase|Tryptase]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 16414069 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16414069}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
2F9O is a 4 chains structure of sequences 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=2F9O OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:16414069</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Tryptase]]
+
[[Category: Large Structures]]
-
[[Category: Bode, W.]]
+
[[Category: Bode W]]
-
[[Category: Huber, R.]]
+
[[Category: Huber R]]
-
[[Category: Marquardt, U.]]
+
[[Category: Marquardt U]]
-
[[Category: Rohr, K B.]]
+
[[Category: Rohr KB]]
-
[[Category: Schechter, N M.]]
+
[[Category: Schechter NM]]
-
[[Category: Selwood, T.]]
+
[[Category: Selwood T]]
-
[[Category: Than, M E.]]
+
[[Category: Than ME]]
-
[[Category: Difucosylation]]
+
-
[[Category: Serine proteinase]]
+
-
[[Category: Trypsin-like]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:35:33 2009''
+

Current revision

Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G

PDB ID 2f9o

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/2f9o"
Personal tools