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PMID: 8662510 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C.

Science (New York, N.Y.) ·Vol. 273 ·No. 5272 ·1996-07-12 ·Pages 248-51

Shao X, Davletov BA, Sutton RB, Südhof TC, Rizo J

Abstract

C2 domains are found in many proteins involved in membrane traffic or signal transduction. Although C2 domains are thought to bind calcium ions, the structural basis for calcium binding is unclear. Analysis of calcium binding to C2 domains of synaptotagmin I and protein kinase C-beta by nuclear magnetic resonance spectroscopy revealed a bipartite calcium-binding motif that involves the coordination of two calcium ions by five aspartate residues located on two separate loops. Sequence comparisons indicated that this may be a widely used calcium-binding motif, designated here as the C2 motif.

MeSH Terms
Aspartic Acid/chemistry Base Sequence Calcium/metabolism Calcium-Binding Proteins Crystallography, X-Ray Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Membrane Glycoproteins/chemistry,metabolism Models, Molecular Molecular Sequence Data Nerve Tissue Proteins/chemistry,metabolism Phospholipids/metabolism Protein Conformation Protein Folding Protein Kinase C/chemistry,metabolism Protein Structure, Secondary Protein Structure, Tertiary Synaptotagmin I Synaptotagmins Temperature
Chemicals
Calcium-Binding Proteins Membrane Glycoproteins Nerve Tissue Proteins Phospholipids Synaptotagmin I Synaptotagmins Aspartic Acid Protein Kinase C Calcium
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Shao X
Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235, USA.
Davletov B A
Sutton R B
Südhof T C
Rizo J
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1996-07-12
Pages
248-51
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIMH NIH HHS · R01-MH52804-01 · United States
NINDS NIH HHS · R29 NS33731-01A1 · United States
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