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Interactions between SH2 and SH3 domains

Vihinen, Mauno LU and Smith, CIE (1998) In Biochemical and Biophysical Research Communications 242(2). p.351-356
Abstract
Src homology 2 (SH2) and SH3 domains are abundant protein and peptide binding modules in signalling molecules. Certain SH2 and SH3 domains have been shown to form functional and physical interactions. The structural basis of dimer formation was studied by docking three dimensional structures of the domains and by analysing structural and functional properties of the dimers. The experimentally verified dimers were noticed to have very large buried surfaces, extensive hydrogen bonding networks, and complementary surfaces, properties which are characteristic for protein-protein interactions. The number of hydrogen bonds between the domains is exceptionally high for interacting protein pairs. Also the buried accessible surface is large,... (More)
Src homology 2 (SH2) and SH3 domains are abundant protein and peptide binding modules in signalling molecules. Certain SH2 and SH3 domains have been shown to form functional and physical interactions. The structural basis of dimer formation was studied by docking three dimensional structures of the domains and by analysing structural and functional properties of the dimers. The experimentally verified dimers were noticed to have very large buried surfaces, extensive hydrogen bonding networks, and complementary surfaces, properties which are characteristic for protein-protein interactions. The number of hydrogen bonds between the domains is exceptionally high for interacting protein pairs. Also the buried accessible surface is large, especially when considering the small size of the domains. The dimer results were used to describe mutation information in structural terms and to discuss regulation of protein tyrosine kinases. (C) 1998 Academic Press. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
242
issue
2
pages
351 - 356
publisher
Elsevier
external identifiers
  • wos:000071496100021
  • scopus:0032515338
ISSN
1090-2104
DOI
10.1006/bbrc.1997.7909
language
English
LU publication?
no
id
a20dd8ba-856f-4902-99cd-ac494c8e5f1b (old id 3852652)
date added to LUP
2013-06-28 14:29:55
date last changed
2017-01-01 06:36:45
@article{a20dd8ba-856f-4902-99cd-ac494c8e5f1b,
  abstract     = {Src homology 2 (SH2) and SH3 domains are abundant protein and peptide binding modules in signalling molecules. Certain SH2 and SH3 domains have been shown to form functional and physical interactions. The structural basis of dimer formation was studied by docking three dimensional structures of the domains and by analysing structural and functional properties of the dimers. The experimentally verified dimers were noticed to have very large buried surfaces, extensive hydrogen bonding networks, and complementary surfaces, properties which are characteristic for protein-protein interactions. The number of hydrogen bonds between the domains is exceptionally high for interacting protein pairs. Also the buried accessible surface is large, especially when considering the small size of the domains. The dimer results were used to describe mutation information in structural terms and to discuss regulation of protein tyrosine kinases. (C) 1998 Academic Press.},
  author       = {Vihinen, Mauno and Smith, CIE},
  issn         = {1090-2104},
  language     = {eng},
  number       = {2},
  pages        = {351--356},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Interactions between SH2 and SH3 domains},
  url          = {http://dx.doi.org/10.1006/bbrc.1997.7909},
  volume       = {242},
  year         = {1998},
}