1h4w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:17, 13 December 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1h4w.png|left|200px]]
 
-
<!--
+
==Structure of human trypsin IV (brain trypsin)==
-
The line below this paragraph, containing "STRUCTURE_1h4w", creates the "Structure Box" on the page.
+
<StructureSection load='1h4w' size='340' side='right'caption='[[1h4w]], [[Resolution|resolution]] 1.70&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'>[[1h4w]] 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=1H4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4W 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]] 1.7&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-
{{STRUCTURE_1h4w| PDB=1h4w | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4w OCA], [https://pdbe.org/1h4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4w RCSB], [https://www.ebi.ac.uk/pdbsum/1h4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4w ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRY3_HUMAN TRY3_HUMAN] Digestive protease specialized for the degradation of trypsin inhibitors. In the ileum, may be involved in defensin processing, including DEFA5.<ref>PMID:12021776</ref> <ref>PMID:14507909</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/h4/1h4w_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=1h4w ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Severe neurodegradative brain diseases, like Alzheimer, are tightly linked with proteolytic activity in the human brain. Proteinases expressed in the brain, such as human trypsin IV, are likely to be involved in the pathomechanism of these diseases. The observation of amyloid formed in the brain of transgenic mice expressing human trypsin IV supports this hypothesis. Human trypsin IV is also resistant towards all studied naturally occurring polypeptide inhibitors. It has been postulated that the substitution of Gly193 to arginine is responsible for this inhibitor resistance. Here we report the X-ray structure of human trypsin IV in complex with the inhibitor benzamidine at 1.7 A resolution. The overall fold of human trypsin IV is similar to human trypsin I, with a root-mean square deviation of only 0.5 A for all C(alpha) positions. The crystal structure reveals the orientation of the side-chain of Arg193, which occupies an extended conformation and fills the S2' subsite. An analysis of surface electrostatic potentials shows an unusually strong clustering of positive charges around the primary specificity pocket, to which the side-chain of Arg193 also contributes. These unique features of the crystal structure provide a structural basis for the enhanced inhibitor resistance, and enhanced substrate restriction, of human trypsin IV.
-
===STRUCTURE OF HUMAN TRYPSIN IV (BRAIN TRYPSIN)===
+
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin.,Katona G, Berglund GI, Hajdu J, Graf L, Szilagyi L J Mol Biol. 2002 Feb 1;315(5):1209-18. PMID:11827488<ref>PMID:11827488</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1h4w" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_11827488}}, adds the Publication Abstract to the page
+
*[[Trypsin 3D structures|Trypsin 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 11827488 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_11827488}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1H4W 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=1H4W OCA].
+
-
 
+
-
==Reference==
+
-
Crystal structure reveals basis for the inhibitor resistance of human brain trypsin., Katona G, Berglund GI, Hajdu J, Graf L, Szilagyi L, J Mol Biol. 2002 Feb 1;315(5):1209-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11827488 11827488]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Trypsin]]
+
[[Category: Berglund GI]]
-
[[Category: Berglund, G I.]]
+
[[Category: Graf L]]
-
[[Category: Graf, L.]]
+
[[Category: Hajdu J]]
-
[[Category: Hajdu, J.]]
+
[[Category: Katona G]]
-
[[Category: Katona, G.]]
+
[[Category: Szilagyi L]]
-
[[Category: Szilagyi, L.]]
+
-
[[Category: Alzheimer disease]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Inhibitor resistance]]
+
-
[[Category: Serine protease]]
+
-
[[Category: Signal transduction]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:37:49 2008''
+

Current revision

Structure of human trypsin IV (brain trypsin)

PDB ID 1h4w

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools