Intertwined structured and unstructured regions of exRAGE identified by monitoring hydrogen-deuterium exchange.
Receptor for advanced glycation end products (RAGE) is a multiligand receptor that is engaged in many pathological processes. Potentially beneficial modification of its activity requires sound knowledge of its structural properties. However, up to now, only the structures of its separated domains have been published or deposited in databases. In this work, we used hydrogen-deuterium exchange and mass spectrometry to gain insight into the structural properties of exRAGE (extracellular region of RAGE)--the full extracellular part of the protein. The present work indicates the common and disparate features of full exRAGE as compared to the structural models of its separate domains. The highlight of the present study is the contrasting behavior of the different regions of the protein, with the protected regions neighboring fully exposed parts especially in the N-terminal V domain.
Kupniewska-Kozak
Anna
A
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland.
Gospodarska
Emilia
E
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland.
Dadlez
Michal
M
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland; Institute of Genetics and Biotechnology, Biology Department, Warsaw University, Miecznikowa 1, 02-185 Warsaw, Poland. Electronic address: michald@ibb.waw.pl.
D000595:Amino Acid Sequence; D003903:Deuterium / Q000032:analysis; D006801:Humans; D006859:Hydrogen / Q000032:analysis; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D000067759:Receptor for Advanced Glycation End Products / Q000737:chemistry*
D000067759:Receptor for Advanced Glycation End Products; D006859:Hydrogen; D003903:Deuterium