1UQV

SAM domain from Ste50p

1UQV の概要

• エントリーDOI: 10.2210/pdb1uqv/pdb
• 分子名称: STE50 PROTEIN (1 entity in total)
• 機能のキーワード: sam, sterile alpha motif, helical, protein-protein interaction domain, growth arrest, signaling protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9897.15

構造登録者

Grimshaw, S.J.,Mott, H.R.,Stott, K.M.,Nielsen, P.R.,Evetts, K.A.,Hopkins, L.J.,Nietlispach, D.,Owen, D. (登録日: 2003-10-20, 公開日: 2003-10-30, 最終更新日: 2024-05-15)

主引用文献

Grimshaw, S.J.,Mott, H.R.,Stott, K.M.,Nielsen, P.R.,Evetts, K.A.,Hopkins, L.J.,Nietlispach, D.,Owen, D.
Structure of the Sterile {Alpha} Motif (Sam) Domain of the Saccharomyces Cerevisiae Mitogen-Activated Protein Kinase Pathway-Modulating Protein Ste50 and Analysis of its Interaction with the Ste11 Sam
J.Biol.Chem., 279:2192-, 2004

PubMed Abstract: The sterile alpha motif (SAM) is a 65-70-amino acid domain found in over 300 proteins that are involved in either signal transduction or transcriptional activation and repression. SAM domains have been shown to mediate both homodimerization and heterodimerization and in some cases oligomerization. Here, we present the solution structure of the SAM domain of the Saccharomyces cerevisiae protein, Ste50p. Ste50p functions as a modulator of the mitogen-activated protein kinase (MAPK) cascades in S. cerevisiae, which control mating, pseudohyphal growth, and osmo-tolerance. This is the first example of the structure of a SAM domain from a MAPK module protein. We have studied the associative behavior of Ste50p SAM in solution and shown that it is monomeric. We have examined the SAM domain from Ste11p, the MAPK kinase kinase that associates with Ste50p in vivo, and shown that it forms dimers with a self-association K(d) of approximately 0.5 mm. We have also analyzed the interaction of Ste50p SAM with Ste11p SAM and the effects of mutations at Val-37, Asp-38, Pro-71, Leu-73, Leu-75, and Met-99 of STE50 on the heterodimerization properties of Ste50p SAM. We have found that L73A and L75A abrogate the Ste50p interaction with Ste11p, and we compare these data with the known interaction sites defined for other SAM domain interactions.

PubMed: 14573615
DOI: 10.1074/JBC.M305605200

実験手法

SOLUTION NMR