3PLS
RON in complex with ligand AMP-PNP
Summary for 3PLS
Entry DOI | 10.2210/pdb3pls/pdb |
Descriptor | Macrophage-stimulating protein receptor, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
Functional Keywords | protein kinase, cis autophosphorylation conformation, receptor tyrosine kinase, amp-pnp, unphosphorylated, single-span transmembrane receptor, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Membrane; Single-pass type I membrane protein: Q04912 |
Total number of polymer chains | 1 |
Total formula weight | 34778.92 |
Authors | Wang, J.,Steinbacher, S.,Augustin, M.,Schreiner, P.,Epstein, D.,Mulvihill, M.J.,Crew, A.P. (deposition date: 2010-11-15, release date: 2010-11-24, Last modification date: 2024-02-21) |
Primary citation | Wang, J.,Steinbacher, S.,Augustin, M.,Schreiner, P.,Epstein, D.,Mulvihill, M.J.,Crew, A.P. The Crystal Structure of a Constitutively Active Mutant RON Kinase Suggests an Intramolecular Autophosphorylation Hypothesis Biochemistry, 49:7972-7974, 2010 Cited by PubMed Abstract: A complex of RON(M1254T) with AMP-PNP and Mg(2+) reveals a substratelike positioning of Tyr1238 as well as likely catalysis-competent placement of the AMP-PNP and Mg(2+) components and indicates a tendency for cis phosphorylation. The structure shows how the oncogenic mutation may cause the constitutive activation and suggests a mechanistic hypothesis for the autophosphorylation of receptor tyrosine kinases. PubMed: 20726546PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.24 Å) |
Structure validation
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