|
|
| Line 1: |
Line 1: |
| [[Image:2asu.gif|left|200px]] | | {{Seed}} |
| | [[Image:2asu.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2asu| PDB=2asu | SCENE= }} | | {{STRUCTURE_2asu| PDB=2asu | SCENE= }} |
|
| |
|
| '''Crystal Structure of the beta-chain of HGFl/MSP'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16279944}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16279944 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_16279944}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| [[Category: Msp]] | | [[Category: Msp]] |
| [[Category: Serine proteinase]] | | [[Category: Serine proteinase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:26:20 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:40:37 2008'' |
