1vzj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
===STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX===
===STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX===
{{ABSTRACT_PUBMED_15526038}}
{{ABSTRACT_PUBMED_15526038}}
 +
 +
==Disease==
 +
[[http://www.uniprot.org/uniprot/COLQ_HUMAN COLQ_HUMAN]] Defects in COLQ are the cause of congenital myasthenic syndrome Engel type (CMSE) [MIM:[http://omim.org/entry/603034 603034]]; also known as end-plate acetylcholinesterase deficiency or congenital myasthenic syndrome type IC (CMS-IC). CMSE is a rare autosomal recessive congenital myasthenic syndrome characterized by onset during childhood, generalized weakness, abnormal fatigability on exertion, refrectoriness to acetylcholinesterase drugs, decremental electromyographic response and morphological abnormalities of the neuromuscular junctions.<ref>PMID:9758617</ref><ref>PMID:10665486</ref>
 +
 +
==Function==
 +
[[http://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref><ref>PMID:1748670</ref><ref>PMID:1517212</ref><ref>PMID:11985878</ref> [[http://www.uniprot.org/uniprot/COLQ_HUMAN COLQ_HUMAN]] Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
==About this Structure==
==About this Structure==
Line 11: Line 17:
==Reference==
==Reference==
-
<ref group="xtra">PMID:015526038</ref><references group="xtra"/>
+
<ref group="xtra">PMID:015526038</ref><references group="xtra"/><references/>
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Bon, S.]]
[[Category: Bon, S.]]

Revision as of 18:35, 24 March 2013

Template:STRUCTURE 1vzj

Contents

STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX

Template:ABSTRACT PUBMED 15526038

Disease

[COLQ_HUMAN] Defects in COLQ are the cause of congenital myasthenic syndrome Engel type (CMSE) [MIM:603034]; also known as end-plate acetylcholinesterase deficiency or congenital myasthenic syndrome type IC (CMS-IC). CMSE is a rare autosomal recessive congenital myasthenic syndrome characterized by onset during childhood, generalized weakness, abnormal fatigability on exertion, refrectoriness to acetylcholinesterase drugs, decremental electromyographic response and morphological abnormalities of the neuromuscular junctions.[1][2]

Function

[ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.[3][4][5][6] [COLQ_HUMAN] Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.

About this Structure

1vzj is a 10 chain structure. Full crystallographic information is available from OCA.

See Also

Reference

  • Dvir H, Harel M, Bon S, Liu WQ, Vidal M, Garbay C, Sussman JL, Massoulie J, Silman I. The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. EMBO J. 2004 Nov 10;23(22):4394-405. Epub 2004 Nov 4. PMID:15526038 doi:7600425
  1. ↑ Donger C, Krejci E, Serradell AP, Eymard B, Bon S, Nicole S, Chateau D, Gary F, Fardeau M, Massoulie J, Guicheney P. Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with end-plate acetylcholinesterase deficiency (Type Ic). Am J Hum Genet. 1998 Oct;63(4):967-75. PMID:9758617
  2. ↑ Ohno K, Engel AG, Brengman JM, Shen XM, Heidenreich F, Vincent A, Milone M, Tan E, Demirci M, Walsh P, Nakano S, Akiguchi I. The spectrum of mutations causing end-plate acetylcholinesterase deficiency. Ann Neurol. 2000 Feb;47(2):162-70. PMID:10665486
  3. ↑ Chhajlani V, Derr D, Earles B, Schmell E, August T. Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. PMID:2714437
  4. ↑ Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A. The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. PMID:1748670
  5. ↑ Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.. Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. PMID:1517212
  6. ↑ Yang L, He HY, Zhang XJ. Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells. Neurosci Res. 2002 Apr;42(4):261-8. PMID:11985878

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vzj"
Personal tools