Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex
Niemann H, Gherardi E, Bleymüller W, Heinz DW (2012)
Protein Science 21(10): 1528-1539.
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Abstract / Bemerkung
The physiological relevance of contacts in crystal lattices often remains elusive. This was also the case for the complex between the invasion protein internalin B (InlB) from Listeria monocytogenes and its host cell receptor, the human receptor tyrosine kinase (RTK) MET. InlB is a MET agonist and induces bacterial host cell invasion. Activation of RTKs generally involves ligand-induced dimerization of the receptor ectodomain. The two currently available crystal structures of the InlB:MET complex show the same arrangement of InlB and MET in a 1:1 complex, but different dimeric 2:2 assemblies. Only one of these 2:2 assemblies is predicted to be stable by a computational procedure. This assembly is mainly stabilized by a contact between the Cap domain of InlB from one and the Sema domain of MET from another 1:1 complex. Here, we probe the physiological relevance of this interaction. We generated variants of the leucine-rich repeat (LRR) protein InlB by inserting an additional repeat between the first and the second LRR. This should allow formation of the 1:1 complex but disrupt the potential 2:2 complex involving the Cap-Sema contact due to steric distortions. A crystal structure of one of the engineered proteins showed that it folded properly. Binding affinity to MET was comparable to that of wild-type InlB. The InlB variant induced MET phosphorylation and cell scatter like wild-type InlB. These results suggest that the Cap-Sema interaction is not physiologically relevant and support the previously proposed assembly, in which a 2:2 InlB:MET complex is built around a ligand dimer. Copyright 2012 The Protein Society.
Erscheinungsjahr
2012
Zeitschriftentitel
Protein Science
Band
21
Ausgabe
10
Seite(n)
1528-1539
ISSN
0961-8368
Page URI
https://pub.uni-bielefeld.de/record/2529531
Zitieren
Niemann H, Gherardi E, Bleymüller W, Heinz DW. Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex. Protein Science. 2012;21(10):1528-1539.
Niemann, H., Gherardi, E., Bleymüller, W., & Heinz, D. W. (2012). Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex. Protein Science, 21(10), 1528-1539. doi:10.1002/pro.2142
Niemann, Hartmut, Gherardi, Ermanno, Bleymüller, Willem, and Heinz, Dirk W. 2012. “Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex”. Protein Science 21 (10): 1528-1539.
Niemann, H., Gherardi, E., Bleymüller, W., and Heinz, D. W. (2012). Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex. Protein Science 21, 1528-1539.
Niemann, H., et al., 2012. Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex. Protein Science, 21(10), p 1528-1539.
H. Niemann, et al., “Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex”, Protein Science, vol. 21, 2012, pp. 1528-1539.
Niemann, H., Gherardi, E., Bleymüller, W., Heinz, D.W.: Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex. Protein Science. 21, 1528-1539 (2012).
Niemann, Hartmut, Gherardi, Ermanno, Bleymüller, Willem, and Heinz, Dirk W. “Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex”. Protein Science 21.10 (2012): 1528-1539.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
PDB
1 Eintrag gefunden, die diesen Artikel zitieren
x-ray diffraction (PDB: 4aw4)
Protein structure name: engineered variant of listeria monocytogenes inlb internalin domain with an additional leucine rich repeat inserted
Public wwPDB file in PDB format
Protein structure name: engineered variant of listeria monocytogenes inlb internalin domain with an additional leucine rich repeat inserted
Public wwPDB file in PDB format
UNIPROT
28 Einträge gefunden, die diesen Artikel zitieren von denen 10 angezeigt werden
Internalin B (UNIPROT: P25147)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Download in FASTA format
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Download in FASTA format
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