NDLI: Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5.

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Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5.

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Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fox, R. O. Lim, W. A. Richards, F. M.
Description	Author Affiliation: Lim WA ( Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.)
Abstract	We have determined the thermodynamic stability and peptide binding affinity of the carboxy-terminal Src homology 3 (SH3) domain from the Caenorhabditis elegans signal-transduction protein Sem-5. Despite its small size (62 residues) and lack of disulfide bonds, this domain is highly stable to thermal denaturation--at pH 7.3, the protein has a Tm of 73.1 degrees C. Interestingly, the protein is not maximally stable at neutral pH, but reaches a maximum at around pH 4.7 (Tm approximately equal to 80 degrees C). Increasing ionic strength also stabilizes the protein, suggesting that 1 or more carboxylate ions are involved in a destabilizing electrostatic interaction. By guanidine hydrochloride denaturation, the protein is calculated to have a free energy of unfolding of 4.1 kcal/mol at 25 degrees C. We have also characterized binding of the domain to 2 different length proline-rich peptides from the guanine nucleotide exchange factor, Sos, one of Sem-5's likely physiological ligands in cytoplasmic signal transduction. Upon binding, these peptides cause about a 2-fold increase in fluorescence intensity. Both bind with only modest affinities (Kd approximately equal to 30 microM), lower than some previous estimates for SH3 domains. By fluorescence, the domain also appears to associate with the homopolymer poly-L-proline in a similar fashion.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	8
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Caenorhabditis Elegans Proteins Caenorhabditis Elegans Chemistry Disulfides Metabolism Helminth Proteins Peptides Signal Transduction Amino Acid Sequence Animals Binding Sites Drug Stability Electrochemistry Guanidine Guanidines Pharmacology Hot Temperature Hydrogen-ion Concentration Molecular Sequence Data Osmolar Concentration Protein Denaturation Protein Folding Thermodynamics Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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