2any: Difference between revisions

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-{{Seed}}
-[[Image:2any.png|left|200px]]
-<!--
+==Expression, Crystallization and the Three-dimensional Structure of the Catalytic Domain of Human Plasma Kallikrein: Implications for Structure-Based Design of Protease Inhibitors==
-The line below this paragraph, containing "STRUCTURE_2any", creates the "Structure Box" on the page.
+<StructureSection load='2any' size='340' side='right'caption='[[2any]], [[Resolution|resolution]] 1.40&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'>[[2any]] 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=2ANY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANY 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]] 1.4&#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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-{{STRUCTURE_2any|  PDB=2any  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2any FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2any OCA], [https://pdbe.org/2any PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2any RCSB], [https://www.ebi.ac.uk/pdbsum/2any PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2any ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/KLKB1_HUMAN KLKB1_HUMAN] Defects in KLKB1 are the cause of prekallikrein deficiency (PKK deficiency) [MIM:[https://omim.org/entry/612423 612423]; also known as Fletcher factor deficiency. This disorder is a blood coagulation defect.
+== Function ==
+[https://www.uniprot.org/uniprot/KLKB1_HUMAN KLKB1_HUMAN] The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin.
+== 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/an/2any_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2any ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Plasma kallikrein is a serine protease that has many important functions, including modulation of blood pressure, complement activation, and mediation and maintenance of inflammatory responses. Although plasma kallikrein has been purified for 40 years, its structure has not been elucidated. In this report, we described two systems (Pichia pastoris and baculovirus/Sf9 cells) for expression of the protease domain of plasma kallikrein, along with the purification and high resolution crystal structures of the two recombinant forms. In the Pichia pastoris system, the protease domain was expressed as a heterogeneously glycosylated zymogen that was activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase to reduce heterogeneity from the glycosylation. The resulting protein was chromatographically resolved into four components, one of which was crystallized. In the baculovirus/Sf9 system, homogeneous, crystallizable, and nonglycosylated protein was expressed after mutagenizing three asparagines (the glycosylation sites) to glutamates. When assayed against the peptide substrates, pefachrome-PK and oxidized insulin B chain, both forms of the protease domain were found to have catalytic activity similar to that of the full-length protein. Crystallization and x-ray crystal structure determination of both forms have yielded the first three-dimensional views of the catalytic domain of plasma kallikrein. The structures, determined at 1.85 A for the endoglycosidase H-deglycosylated protease domain produced from P. pastoris and at 1.40 A for the mutagenically deglycosylated form produced from Sf9 cells, show that the protease domain adopts a typical chymotrypsin-like serine protease conformation. The structural information provides insights into the biochemical and enzymatic properties of plasma kallikrein and paves the way for structure-based design of protease inhibitors that are selective either for or against plasma kallikrein.
-===Expression, Crystallization and the Three-dimensional Structure of the Catalytic Domain of Human Plasma Kallikrein: Implications for Structure-Based Design of Protease Inhibitors===
+Expression, crystallization, and three-dimensional structure of the catalytic domain of human plasma kallikrein.,Tang J, Yu CL, Williams SR, Springman E, Jeffery D, Sprengeler PA, Estevez A, Sampang J, Shrader W, Spencer J, Young W, McGrath M, Katz BA J Biol Chem. 2005 Dec 9;280(49):41077-89. Epub 2005 Sep 30. PMID:16199530<ref>PMID:16199530</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2any" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16199530}}, adds the Publication Abstract to the page
+*[[Kallikrein 3D structures|Kallikrein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16199530 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16199530}}
+__TOC__
+</StructureSection>
-==About this Structure==
-ANY 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=2ANY OCA].
-==Reference==
-Expression, crystallization, and three-dimensional structure of the catalytic domain of human plasma kallikrein., Tang J, Yu CL, Williams SR, Springman E, Jeffery D, Sprengeler PA, Estevez A, Sampang J, Shrader W, Spencer J, Young W, McGrath M, Katz BA, J Biol Chem. 2005 Dec 9;280(49):41077-89. Epub 2005 Sep 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16199530 16199530]
 [[Category: Homo sapiens]]
-[[Category: Plasma kallikrein]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Estevez A]]
-[[Category: Estevez, A.]]
+[[Category: Jeffery D]]
-[[Category: Jeffery, D.]]
+[[Category: Katz BA]]
-[[Category: Katz, B A.]]
+[[Category: McGrath ME]]
-[[Category: McGrath, M E.]]
+[[Category: Sampang J]]
-[[Category: Sampang, J.]]
+[[Category: Shrader W]]
-[[Category: Shrader, W.]]
+[[Category: Spencer JR]]
-[[Category: Spencer, J R.]]
+[[Category: Sprengeler PA]]
-[[Category: Sprengeler, P A.]]
+[[Category: Springman E]]
-[[Category: Springman, E.]]
+[[Category: Tang J]]
-[[Category: Tang, J.]]
+[[Category: Williams SR]]
-[[Category: Williams, S R.]]
+[[Category: Young WB]]
-[[Category: Young, W B.]]
+[[Category: Yu CL]]
-[[Category: Yu, C L.]]
-[[Category: Mutagenically deglycosyalted human plasma kallikrein protease domain]]
-[[Category: Trypsin-like serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:53:32 2008''