Hostname: page-component-cd9895bd7-hc48f Total loading time: 0 Render date: 2024-12-26T14:15:08.964Z Has data issue: false hasContentIssue false
  • English
  • Français

Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations

Published online by Cambridge University Press:  01 January 2000

I. TSIGELNY ,
I.N. SHINDYALOV ,
P.E. BOURNE ,
T.C. SÜDHOF  and
P. TAYLOR
I. TSIGELNY
Affiliation:
Department of Pharmacology, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093
I.N. SHINDYALOV
Affiliation:
San Diego Supercomputer Center, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093
P.E. BOURNE
Affiliation:
Department of Pharmacology, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093 San Diego Supercomputer Center, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093
T.C. SÜDHOF
Affiliation:
Center for Basic Neuroscience, Department of Molecular Genetics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75235
P. TAYLOR
Affiliation:
Department of Pharmacology, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093
Get access

Abstract

Comparisons of protein sequence via cyclic training of Hidden Markov Models (HMMs) in conjunction with alignments of three-dimensional structure, using the Combinatorial Extension (CE) algorithm, reveal two putative EF-hand metal binding domains in acetylcholinesterase. Based on sequence similarity, putative EF-hands are also predicted for the neuroligin family of cell surface proteins. These predictions are supported by experimental evidence. In the acetylcholinesterase crystal structure from Torpedo californica, the first putative EF-hand region binds the Zn2+ found in the heavy metal replacement structure. Further, the interaction of neuroligin 1 with its cognate receptor neurexin depends on Ca2+. Thus, members of the α,β hydrolase fold family of proteins contain potential Ca2+ binding sites, which in some family members may be critical for heterologous cell associations.

Keywords

acetylcholinesteraseCombinatorial Extension (CE) algorithmEF-handHidden Markov Models (HMM)neuroligin
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 1 , January 2000 , pp. 180 - 185
Copyright
© 2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)