2uzx
From Proteopedia
(New page: 200px<br /> <applet load="2uzx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2uzx, resolution 2.8Å" /> '''STRUCTURE OF THE HUM...) |
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caption="2uzx, resolution 2.8Å" /> | caption="2uzx, resolution 2.8Å" /> | ||
'''STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: CRYSTAL FORM I'''<br /> | '''STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: CRYSTAL FORM I'''<br /> | ||
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==Overview== | ==Overview== | ||
The tyrosine kinase Met, the product of the c-met proto-oncogene and the, receptor for hepatocyte growth factor/scatter factor (HGF/SF), mediates, signals critical for cell survival and migration. The human pathogen, Listeria monocytogenes exploits Met signaling for invasion of host cells, via its surface protein InlB. We present the crystal structure of the, complex between a large fragment of the human Met ectodomain and the, Met-binding domain of InlB. The concave face of the InlB leucine-rich, repeat region interacts tightly with the first immunoglobulin-like domain, of the Met stalk, a domain which does not bind HGF/SF. A second contact, between InlB and the Met Sema domain locks the otherwise flexible receptor, in a rigid, signaling competent conformation. Full Met activation requires, the additional C-terminal domains of InlB which induce heparin-mediated, receptor clustering and potent signaling. Thus, although it elicits a, similar cellular response, InlB is not a structural mimic of HGF/SF. | The tyrosine kinase Met, the product of the c-met proto-oncogene and the, receptor for hepatocyte growth factor/scatter factor (HGF/SF), mediates, signals critical for cell survival and migration. The human pathogen, Listeria monocytogenes exploits Met signaling for invasion of host cells, via its surface protein InlB. We present the crystal structure of the, complex between a large fragment of the human Met ectodomain and the, Met-binding domain of InlB. The concave face of the InlB leucine-rich, repeat region interacts tightly with the first immunoglobulin-like domain, of the Met stalk, a domain which does not bind HGF/SF. A second contact, between InlB and the Met Sema domain locks the otherwise flexible receptor, in a rigid, signaling competent conformation. Full Met activation requires, the additional C-terminal domains of InlB which induce heparin-mediated, receptor clustering and potent signaling. Thus, although it elicits a, similar cellular response, InlB is not a structural mimic of HGF/SF. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Autism, suseptibility to, 9 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164860 164860]], Hepatocellular carcinoma, childhood type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164860 164860]], Renal cell carcinoma, papillary, familial and sporadic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164860 164860]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2UZX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http:// | + | 2UZX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UZX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: virulence factor]] | [[Category: virulence factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:18:46 2008'' |
Revision as of 12:18, 23 January 2008
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STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: CRYSTAL FORM I
Overview
The tyrosine kinase Met, the product of the c-met proto-oncogene and the, receptor for hepatocyte growth factor/scatter factor (HGF/SF), mediates, signals critical for cell survival and migration. The human pathogen, Listeria monocytogenes exploits Met signaling for invasion of host cells, via its surface protein InlB. We present the crystal structure of the, complex between a large fragment of the human Met ectodomain and the, Met-binding domain of InlB. The concave face of the InlB leucine-rich, repeat region interacts tightly with the first immunoglobulin-like domain, of the Met stalk, a domain which does not bind HGF/SF. A second contact, between InlB and the Met Sema domain locks the otherwise flexible receptor, in a rigid, signaling competent conformation. Full Met activation requires, the additional C-terminal domains of InlB which induce heparin-mediated, receptor clustering and potent signaling. Thus, although it elicits a, similar cellular response, InlB is not a structural mimic of HGF/SF.
About this Structure
2UZX is a Protein complex structure of sequences from Homo sapiens and Listeria monocytogenes. Full crystallographic information is available from OCA.
Reference
Structure of the Human Receptor Tyrosine Kinase Met in Complex with the Listeria Invasion Protein InlB., Niemann HH, Jager V, Butler PJ, van den Heuvel J, Schmidt S, Ferraris D, Gherardi E, Heinz DW, Cell. 2007 Jul 27;130(2):235-246. PMID:17662939
Page seeded by OCA on Wed Jan 23 14:18:46 2008
Categories: Homo sapiens | Listeria monocytogenes | Protein complex | Butler, P.J.G. | Ferraris, D. | Gherardi, E. | Heinz, D.W. | Heuvel, J.Van.Den. | Jager, V. | Niemann, H.H. | Schmidt, S. | Alternative splicing | Atp-binding | Chromosomal rearrangement | Disease mutation | Glycoprotein | Hepatocyte growth factor receptor | Hgfr | Internalin | Kinase | Leucine rich repeat | Leucine-rich repeat | Lrr | Membrane | Nucleotide-binding | Phosphorylation | Polymorphism | Proto-oncogene | Receptor | Receptor ectodomain | Signaling protein | Signaling protein/receptor complex | Transferase | Transmembrane | Tyrosine-protein kinase | Virulence factor
