title: Intraprotein signal transduction by HAMP domains: a balancing act.
abstract: HAMP domains are small protein modules that predominantly operate as signal transducers in bacterial sensor proteins most of which are membrane delimited. The domain organization of such sensors has the HAMPs localized at the intersection between the membrane-anchored input sensor and the cytosolic output machinery. The data summarized here indicate that HAMP modules use a universal signaling language in balancing the communication between diverse membrane-bound input domains and cytosolic output domains that are completely foreign to each other.
authors.affiliation: Pharmazeutische Biochemie, Pharmazeutisches Institut, Universität Tübingen, Auf der Morgenstelle 8, 72076 Tübingen, Germany. Electronic address: joachim.schultz@uni-tuebingen.de.
authors.forename: Joachim E
authors.initials: JE
authors.lastname: Schultz
authors.affiliation: Department of Biochemistry and Molecular Biology, Medical and Health Science Center, University of Debrecen, Debrecen H 4032, Hungary.
authors.forename: Kajal
authors.initials: K
authors.lastname: Kanchan
authors.affiliation: Pharmazeutische Biochemie, Pharmazeutisches Institut, Universität Tübingen, Auf der Morgenstelle 8, 72076 Tübingen, Germany.
authors.forename: Miriam
authors.initials: M
authors.lastname: Ziegler
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins
keywords: Adenylate cyclase; HAMP domain; Membrane receptor; Signaling language