4CIL

YopM-InlB: Hybrid leucine-rich repeat protein

Summary for 4CIL

• Entry DOI: 10.2210/pdb4cil/pdb
• Descriptor: YOPM-CAP, INTERNALIN B (2 entities in total)
• Functional Keywords: signaling protein, capping, fusion protein, lrr, protein chimera, protein design, protein engineering
• Biological source: YERSINIA ENTEROCOLITICA; More
• Total number of polymer chains: 1
• Total formula weight: 32170.66

Authors

Breitsprecher, D.,Niemann, H.H. (deposition date: 2013-12-11, release date: 2014-04-02, Last modification date: 2023-12-20)

Primary citation

Breitsprecher, D.,Gherardi, E.,Bleymuller, W.M.,Niemann, H.H.
Crystal Structure of an Engineered Yopm-Inlb Hybrid Protein.
Bmc Struct.Biol., 14:12-, 2014

PubMed Abstract: The multi-domain protein InlB (internalin B) from Listeria monocytogenes is an agonist of the human receptor tyrosine kinase MET. Only the internalin domain directly interacts with MET. The internalin domain consists of seven central leucine-rich repeats (LRRs) flanked by an N-terminal helical cap domain and a C-terminal immunoglobulin-like structure. A potential function of the N-terminal cap in receptor binding could so far not be demonstrated by deleting the cap, since the cap is also implicated in nucleating folding of the LRR domain.

PubMed: 24669959
DOI: 10.1186/1472-6807-14-12

Experimental method

X-RAY DIFFRACTION (1.5 Å)