2asu

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[[Image:2asu.gif|left|200px]]<br /><applet load="2asu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2asu.gif|left|200px]]
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caption="2asu, resolution 1.85&Aring;" />
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'''Crystal Structure of the beta-chain of HGFl/MSP'''<br />
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{{Structure
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|PDB= 2asu |SIZE=350|CAPTION= <scene name='initialview01'>2asu</scene>, resolution 1.85&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= MST1, HGFL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of the beta-chain of HGFl/MSP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2ASU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] 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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2ASU is a [[Protein complex]] 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].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16279944 16279944]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16279944 16279944]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: serine proteinase]]
[[Category: serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:53:29 2008''

Revision as of 13:53, 20 March 2008


PDB ID 2asu

Drag the structure with the mouse to rotate
, resolution 1.85Å
Gene: MST1, HGFL (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the beta-chain of HGFl/MSP


Overview

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.

About this Structure

2ASU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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