ABCC11 p.Leu95Ala
| Predicted by SNAP2: | A: N (72%), C: N (57%), D: D (80%), E: D (75%), F: N (72%), G: D (66%), H: D (71%), I: N (87%), K: D (71%), M: N (93%), N: D (66%), P: D (71%), Q: D (63%), R: D (71%), S: D (59%), T: N (61%), V: N (82%), W: N (57%), Y: D (66%), |
| Predicted by PROVEAN: | A: N, C: N, D: D, E: D, F: N, G: D, H: D, I: N, K: D, M: N, N: D, P: D, Q: N, R: D, S: N, T: N, V: N, W: D, Y: D, |
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[hide] Analysis of the MRP8-MRP14 protein-protein interac... J Biol Chem. 1999 Jan 1;274(1):183-8. Propper C, Huang X, Roth J, Sorg C, Nacken W
Analysis of the MRP8-MRP14 protein-protein interaction by the two-hybrid system suggests a prominent role of the C-terminal domain of S100 proteins in dimer formation.
J Biol Chem. 1999 Jan 1;274(1):183-8., [PMID:9867828]
Abstract [show]
Calcium-binding S100 proteins are thought to play a central role in calcium-mediated signal transduction pathways. They consist of two helix-loop-helix, calcium-binding EF-hand domains. A characteristic feature is their tendency to form homo- and/or heterodimeric complexes. This report presents for the first time a functional "in vivo" approach to the analysis of S100 protein dimerization. Using the two-hybrid system we analyzed the dimerization of MRP8 (S100A8) and MRP14 (S100A9), two S100 proteins expressed in myeloid cells. It is reported that the MRP8-MRP14 heteromer is the clearly preferred complex in both man and mouse. The ability to homodimerize, however, appears to be restricted to the murine MRPs. Interaction analysis of chimeric murine/human MRP14 proteins indicates, that the C-terminal EF-hand domain plays a prominent role in MRP8-MRP14 interaction and determines the specificity of dimerization. Site-directed mutagenesis of four evolutionary conserved hydrophobic amino acids, which have been recently supposed to be essential for S100 protein dimerization, suggests that at least one of these, namely the most N-terminal located residue, is not critical for dimerization.
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No. Sentence Comment
137 Amino Acid Exchanges of F89A, L95A, and F20A, but Not I17A Abolish Dimerization-Recent publications investigated the dimeric structure of S100 protein calcyclin via NMR spectroscopy (6).
X
ABCC11 p.Leu95Ala 9867828:137:30
status: NEW139 To investigate the functional relevance of these residues several murine MRP14 mutants were constructed by exchanging single amino acids (Fig. 2): phenylalanine at position 89 to alanine (F89A), leucine at position 95 to alanine (I95A), isoleucine at position 17 to alanine (I17A), and phenylalanine at position 20 to alanine (F20A).
X
ABCC11 p.Leu95Ala 9867828:139:195
status: NEW194 Vector encoding GAL4-DNA-BD Vector encoding GAL4-AD mMRP8 mMRP14 beta-GAL units % beta-GAL units % mMRP14 92 Ϯ 20 100 Ϯ 22 28 Ϯ 10 30 Ϯ 11 mMRP8 32 Ϯ 9 35 Ϯ 10 109 Ϯ 17 118 Ϯ 18 mMRP14 (1-101) 37 Ϯ 12 40 Ϯ 13 14 Ϯ 4 15 Ϯ 4 mMRP14 (1-85) Ͻ1 Ͻ1 Ͻ1 Ͻ1 mMRP14 (1-69) Ͻ1 Ͻ1 Ͻ1 Ͻ1 mMRP14 (9-113) 20 Ϯ 9 22 Ϯ 10 12 Ϯ 3 13 Ϯ 3 mMRP14-I17A 23 Ϯ 8 25 Ϯ 9 6 Ϯ 2 7 Ϯ 2 mMRP14-F20A 4 Ϯ 1 4 Ϯ 1 Ͻ1 Ͻ1 mMRP14-F89A 2 Ϯ 1 2 Ϯ 1 Ͻ1 Ͻ1 mMRP14-L95A Ͻ1 Ͻ1 Ͻ1 Ͻ1 mhMRP14 2 Ϯ 1 2 Ϯ 1 Ͻ1 Ͻ1 hmMRP14 64 Ϯ 10 70 Ϯ 11 16 Ϯ 4 17 Ϯ 4 S100A12mMRP14 2 Ϯ 1 2 Ϯ 1 Ͻ1 Ͻ1 S100A12 Ͻ1 Ͻ1 Ͻ1 Ͻ1 Vector encoding GAL4-AD hMRP8 hMRP14 beta-GAL units % beta-GAL units % hMRP14 84 Ϯ 13 100 Ϯ 15 4 Ϯ 1 5 Ϯ 1 hMRP8 7 Ϯ 4 8 Ϯ 5 89 Ϯ 8 106 Ϯ 10 hMRP14-C3S 18 Ϯ 6 21 Ϯ 7 2 Ϯ 1 2 Ϯ 1 hMRP14 (5-114) 16 Ϯ 5 19 Ϯ 6 2 Ϯ 1 2 Ϯ 1 mhMRP14 52 Ϯ 8 58 Ϯ 9 2 Ϯ 1 2 Ϯ 1 hmMRP14 2 Ϯ 1 2 Ϯ 1 3 Ϯ 1 4 Ϯ 1 S100A12mMRP14 Ͻ1 Ͻ1 Ͻ1 Ͻ1 S100A12 Ͻ1 Ͻ1 Ͻ1 Ͻ1 The chimeric human S100A12/murine MRP14 molecule did not dimerize with MRPs in yeast, suggesting that not any N-terminal S100 domain can substitute the homologous one.
X
ABCC11 p.Leu95Ala 9867828:194:640
status: NEW197 The analysis of three of these mutants, F20A, F89A, and L95A, seems to confirm the importance of these residues.
X
ABCC11 p.Leu95Ala 9867828:197:56
status: NEW138 Amino Acid Exchanges of F89A, L95A, and F20A, but Not I17A Abolish Dimerization-Recent publications investigated the dimeric structure of S100 protein calcyclin via NMR spectroscopy (6).
X
ABCC11 p.Leu95Ala 9867828:138:30
status: NEW140 To investigate the functional relevance of these residues several murine MRP14 mutants were constructed by exchanging single amino acids (Fig. 2): phenylalanine at position 89 to alanine (F89A), leucine at position 95 to alanine (I95A), isoleucine at position 17 to alanine (I17A), and phenylalanine at position 20 to alanine (F20A).
X
ABCC11 p.Leu95Ala 9867828:140:195
status: NEW195 Vector encoding GAL4-DNA-BD Vector encoding GAL4-AD mMRP8 mMRP14 b-GAL units % b-GAL units % mMRP14 92 6 20 100 6 22 28 6 10 30 6 11 mMRP8 32 6 9 35 6 10 109 6 17 118 6 18 mMRP14 (1-101) 37 6 12 40 6 13 14 6 4 15 6 4 mMRP14 (1-85) ,1 ,1 ,1 ,1 mMRP14 (1-69) ,1 ,1 ,1 ,1 mMRP14 (9-113) 20 6 9 22 6 10 12 6 3 13 6 3 mMRP14-I17A 23 6 8 25 6 9 6 6 2 7 6 2 mMRP14-F20A 4 6 1 4 6 1 ,1 ,1 mMRP14-F89A 2 6 1 2 6 1 ,1 ,1 mMRP14-L95A ,1 ,1 ,1 ,1 mhMRP14 2 6 1 2 6 1 ,1 ,1 hmMRP14 64 6 10 70 6 11 16 6 4 17 6 4 S100A12mMRP14 2 6 1 2 6 1 ,1 ,1 S100A12 ,1 ,1 ,1 ,1 Vector encoding GAL4-AD hMRP8 hMRP14 b-GAL units % b-GAL units % hMRP14 84 6 13 100 6 15 4 6 1 5 6 1 hMRP8 7 6 4 8 6 5 89 6 8 106 6 10 hMRP14-C3S 18 6 6 21 6 7 2 6 1 2 6 1 hMRP14 (5-114) 16 6 5 19 6 6 2 6 1 2 6 1 mhMRP14 52 6 8 58 6 9 2 6 1 2 6 1 hmMRP14 2 6 1 2 6 1 3 6 1 4 6 1 S100A12mMRP14 ,1 ,1 ,1 ,1 S100A12 ,1 ,1 ,1 ,1 MRP8-MRP14 Interaction Analyzed by the Two-hybrid System The chimeric human S100A12/murine MRP14 molecule did not dimerize with MRPs in yeast, suggesting that not any N-terminal S100 domain can substitute the homologous one.
X
ABCC11 p.Leu95Ala 9867828:195:418
status: NEW198 The analysis of three of these mutants, F20A, F89A, and L95A, seems to confirm the importance of these residues.
X
ABCC11 p.Leu95Ala 9867828:198:56
status: NEW