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2asu

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Revision as of 14:37, 12 October 2017

Crystal Structure of the beta-chain of HGFl/MSP

Structural highlights

2asu is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1bui
Gene:	MST1, HGFL (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Carafoli F, Chirgadze DY, Blundell TL, Gherardi E. Crystal structure of the beta-chain of human hepatocyte growth factor-like/macrophage stimulating protein. FEBS J. 2005 Nov;272(22):5799-807. PMID:16279944 doi:10.1111/j.1742-4658.2005.04968.x

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2asu"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the beta-chain of HGFl/MSP==
 <StructureSection load='2asu' size='340' side='right' caption='[[2asu]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bui|1bui]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MST1, HGFL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2asu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2asu OCA], [http://pdbe.org/2asu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2asu RCSB], [http://www.ebi.ac.uk/pdbsum/2asu PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2asu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2asu OCA], [http://pdbe.org/2asu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2asu RCSB], [http://www.ebi.ac.uk/pdbsum/2asu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2asu ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

2asu

From Proteopedia

Revision as of 14:37, 12 October 2017

Crystal Structure of the beta-chain of HGFl/MSP

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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