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3PLS

RON in complex with ligand AMP-PNP

Summary for 3PLS
Entry DOI10.2210/pdb3pls/pdb
DescriptorMacrophage-stimulating protein receptor, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
Functional Keywordsprotein kinase, cis autophosphorylation conformation, receptor tyrosine kinase, amp-pnp, unphosphorylated, single-span transmembrane receptor, transferase
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Single-pass type I membrane protein: Q04912
Total number of polymer chains1
Total formula weight34778.92
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 citationWang, 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: 20726546
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.24 Å)
Structure validation

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数据于2024-11-06公开中

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