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A predicted consensus structure for the protein kinase C2 homology (C2H) domain, the repeating unit of synaptotagmin
Author(s) -
Gerloff Dietlind L.,
Chelvanayagam Gareth,
Benner Steven A.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220402
Subject(s) - synaptotagmin 1 , protein secondary structure , loop modeling , threading (protein sequence) , beta sheet , protein structure , homology (biology) , protein kinase domain , microbiology and biotechnology , homology modeling , chemistry , biology , protein structure prediction , biophysics , computational biology , biochemistry , enzyme , gene , membrane , vesicle , synaptic vesicle , mutant
A secondary structure has been predicted for the protein kinase C2 regulatory domain found in homologous form in synaptotagmin, some phospholipases, and some GTP activated proteins. The proposed structure is built from seven consecutive beta strands followed by a terminal alpha helix. Considerations of overall surface exposure of individual secondary structural elements suggest that these are packed into a 2‐sheet beta sandwich structure, with one of only three of the many possible folds being preferred. © 1995 Wiley‐Liss, Inc.