NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase

被引:33
作者
Lee, GI
Ding, ZF
Walker, JC
Van Doren, SR
机构
[1] Univ Missouri, Dept Biochem, Columbia, MO 65211 USA
[2] Univ Missouri, Div Biol Sci, Columbia, MO 65211 USA
关键词
D O I
10.1073/pnas.2031918100
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Fork nead-associated (FHA) domains are phosphoprotein-binding modules found in diverse signaling proteins that bind partners phosphorylated on threonine or serine. Kinase-associated protein phosphatase from Arabidopsis employs its FHA domain for negative regulation of receptor-like kinase signaling pathways, which are important in plant development. The solution structure of the free state of kinase-interacting FHA domain (KI-FHA) of kinase-associated protein phosphatase has been determined with high precision and accuracy using residual dipolar couplings. KI-FHA is a sandwich of a five-stranded mixed beta-sheet with a six-stranded antiparallel beta-sheet. Despite homology only in the recognition loop;, this fold is shared with FHA domains from checkpoint proteins from yeast and humans, as well as with nonhomologous MH2 domains of Smad tumor suppressors. A shared pattern of hydrophobicity throughout FHA domains and Smad MH2 domains may stabilize the core of the p-sandwich. Evolutionary trace analysis of FHA domains suggests class-specific residues in the recognition loops that could tune their phosphoprotein-binding specificity. This surface agrees with that of KI-FHA in contact with a phosphothreonine peptide ligand. Evolutionary trace analysis also predicts an unexpected swath of class-specific residues on another face of FHA domains. Protein interactions with these faces may affect assembly of transmembrane signaling complexes in plans, and in other FHA domain-containing assemblies.
引用
收藏
页码:11261 / 11266
页数:6
相关论文
共 48 条
[1]   Automated structure-based prediction of functional sites in proteins: Applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking [J].
Aloy, P ;
Querol, E ;
Aviles, FX ;
Sternberg, MJE .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 311 (02) :395-408
[2]   Receptor kinase signaling in plant development [J].
Becraft, PW .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2002, 18 :163-192
[3]   Interaction of the maize and Arabidopsis kinase interaction domains with a subset of receptor-like protein kinases: Implications for transmembrane signaling in plants [J].
Braun, DM ;
Stone, JM ;
Walker, JC .
PLANT JOURNAL, 1997, 12 (01) :83-95
[4]   Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].
Brunger, AT ;
Adams, PD ;
Clore, GM ;
DeLano, WL ;
Gros, P ;
Grosse-Kunstleve, RW ;
Jiang, JS ;
Kuszewski, J ;
Nilges, M ;
Pannu, NS ;
Read, RJ ;
Rice, LM ;
Simonson, T ;
Warren, GL .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921
[5]   Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: Comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexes [J].
Byeon, IJL ;
Yongkiettrakul, S ;
Tsai, MD .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 314 (03) :577-588
[6]   Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein [J].
Choy, WY ;
Tollinger, M ;
Mueller, GA ;
Kay, LE .
JOURNAL OF BIOMOLECULAR NMR, 2001, 21 (01) :31-40
[7]   A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information [J].
Clore, GM ;
Gronenborn, AM ;
Bax, A .
JOURNAL OF MAGNETIC RESONANCE, 1998, 133 (01) :216-221
[8]   Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase [J].
Cornilescu, G ;
Marquardt, JL ;
Ottiger, M ;
Bax, A .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (27) :6836-6837
[9]   Dimerization of G-protein-coupled receptors [J].
Dean, MK ;
Higgs, C ;
Smith, RE ;
Bywater, RP ;
Snell, CR ;
Scott, PD ;
Upton, GJG ;
Howe, TJ ;
Reynolds, CA .
JOURNAL OF MEDICINAL CHEMISTRY, 2001, 44 (26) :4595-4614
[10]   The FHA domain [J].
Durocher, D ;
Jackson, SP .
FEBS LETTERS, 2002, 513 (01) :58-66