4pxj
From Proteopedia
Crystallographic structure of the LZII fragment (anti-parallel orientation) from JIP3
Structural highlights
FunctionJIP3_HUMAN The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity). Publication Abstract from PubMedJIP3 and JIP4, two highly related scaffolding proteins for MAP kinases, are binding partners for two molecular motors as well as for the small G protein ARF6. The leucine zipper II (LZII) region of JIP3/4 is the binding site for these three partners. Previously, the crystal structure of ARF6 bound to JIP4 revealed LZII in a parallel coiled-coil arrangement. Here, the crystal structure of an N-terminally truncated form of LZII of JIP3 alone shows an unexpected antiparallel arrangement. Using molecular dynamics and modelling, the stability of this antiparallel LZII arrangement, as well as its specificity for ARF6, were investigated. This study highlights that N-terminal truncation of LZII can change its coiled-coil orientation without affecting its overall stability. Further, a conserved buried asparagine residue was pinpointed as a possible structural determinant for this dramatic structural rearrangement. Thus, LZII of JIP3/4 is a versatile structural motif, modifications of which can impact partner recognition and thus biological function. Structure of a truncated form of leucine zipper II of JIP3 reveals an unexpected antiparallel coiled-coil arrangement.,Llinas P, Chenon M, Nguyen TQ, Moreira C, de Regibus A, Coquard A, Ramos MJ, Guerois R, Fernandes PA, Menetrey J Acta Crystallogr F Struct Biol Commun. 2016 Mar;72(Pt 3):198-206. doi:, 10.1107/S2053230X16001576. Epub 2016 Feb 16. PMID:26919523[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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