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2asu

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{{Seed}}
 
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[[Image:2asu.png|left|200px]]
 
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==Crystal Structure of the beta-chain of HGFl/MSP==
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The line below this paragraph, containing "STRUCTURE_2asu", creates the "Structure Box" on the page.
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<StructureSection load='2asu' size='340' side='right'caption='[[2asu]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2asu]] is a 2 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=2ASU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ASU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2asu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2asu OCA], [https://pdbe.org/2asu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2asu RCSB], [https://www.ebi.ac.uk/pdbsum/2asu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2asu ProSAT]</span></td></tr>
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{{STRUCTURE_2asu| PDB=2asu | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HGFL_HUMAN HGFL_HUMAN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/as/2asu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2asu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hepatocyte growth factor like/macrophage stimulating protein (HGFl/MSP) and hepatocyte growth factor/scatter factor (HGF/SF) define a distinct family of vertebrate-specific growth factors structurally related to the blood proteinase precursor plasminogen and with important roles in development and cancer. Although the two proteins share a similar domain structure and mechanism of activation, there are differences between HGFl/MSP and HGF/SF in terms of the contribution of individual domains to receptor binding. Here we present a crystal structure of the 30 kDa beta-chain of human HGFl/MSP, a serine proteinase homology domain containing the high-affinity binding site for the RON receptor. The structure describes at 1.85 Angstrom resolution the region of the domain corresponding to the receptor binding site recently defined in the HGF/SF beta-chain, namely the central cleft harboring the three residues corresponding to the catalytic ones of active proteinases (numbers in brackets define the sequence position according to the standard chymotrypsinogen numbering system) [Gln522 (c57), Gln568 (c102) and Tyr661 (c195)] and an adjacent loop flanking the S1 specificity pocket and containing residues Asn682 (c217) and Arg683 (c218) previously shown to be essential for binding of HGFl/MSP to the RON receptor. The study confirms the concept that the serine proteinase homology domains of HGFl/MSP and HGF/SF bind their receptors in an 'enzyme-substrate' mode, reflecting the common evolutionary origin of the plasminogen-related growth factors and the proteinases of the clotting and fibrinolytic pathways. However, analysis of the intermolecular interactions in the crystal lattice of beta-chain HGFl/MSP fails to show the same contacts seen in the HGF/SF structures and does not support a conserved mode of dimerization of the serine proteinase homology domains of HGFl/MSP and HGF/SF responsible for receptor activation.
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===Crystal Structure of the beta-chain of HGFl/MSP===
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Crystal structure of the beta-chain of human hepatocyte growth factor-like/macrophage stimulating protein.,Carafoli F, Chirgadze DY, Blundell TL, Gherardi E FEBS J. 2005 Nov;272(22):5799-807. PMID:16279944<ref>PMID:16279944</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16279944}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2asu" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16279944 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16279944}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2ASU is a 2 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=2ASU OCA].
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==Reference==
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<ref group="xtra">PMID:16279944</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Blundell, T L.]]
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[[Category: Large Structures]]
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[[Category: Carafoli, F.]]
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[[Category: Blundell TL]]
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[[Category: Chirgadze, D Y.]]
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[[Category: Carafoli F]]
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[[Category: Gherardi, E.]]
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[[Category: Chirgadze DY]]
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[[Category: Beta-chain]]
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[[Category: Gherardi E]]
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[[Category: Hgfl]]
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[[Category: Msp]]
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[[Category: Serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:18:46 2009''
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Current revision

Crystal Structure of the beta-chain of HGFl/MSP

PDB ID 2asu

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