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6cud

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Revision as of 20:49, 6 March 2020

Structure of the human TRPC3 in a lipid-occupied, closed state

6cud, resolution 3.30Å

Structural highlights

6cud is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	TRPC3, TRP3 (HUMAN)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[TRPC3_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.

Function

[TRPC3_HUMAN] Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3. May also be activated by internal calcium store depletion.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

The TRPC channels are crucially involved in store-operated calcium entry and calcium homeostasis, and they are implicated in human diseases such as neurodegenerative disease, cardiac hypertrophy, and spinocerebellar ataxia. We present a structure of the full-length human TRPC3, a lipid-gated TRPC member, in a lipid-occupied, closed state at 3.3 Angstrom. TRPC3 has four elbow-like membrane reentrant helices prior to the first transmembrane helix. The TRP helix is perpendicular to, and thus disengaged from, the pore-lining S6, suggesting a different gating mechanism from other TRP subfamily channels. The third transmembrane helix S3 is remarkably long, shaping a unique transmembrane domain, and constituting an extracellular domain that may serve as a sensor of external stimuli. We identified two lipid binding sites, one being sandwiched between the pre-S1 elbow and the S4-S5 linker, and the other being close to the ion-conducting pore, where the conserved LWF motif of the TRPC family is located.

Structure of the human lipid-gated cation channel TRPC3.,Fan C, Choi W, Sun W, Du J, Lu W Elife. 2018 May 4;7. pii: 36852. doi: 10.7554/eLife.36852. PMID:29726814^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Woo JS, Hwang JH, Ko JK, Weisleder N, Kim DH, Ma J, Lee EH. S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle. Biochem J. 2010 Mar 15;427(1):125-34. doi: 10.1042/BJ20091225. PMID:20095964 doi:http://dx.doi.org/10.1042/BJ20091225
↑ Zhu X, Jiang M, Peyton M, Boulay G, Hurst R, Stefani E, Birnbaumer L. trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry. Cell. 1996 May 31;85(5):661-71. PMID:8646775
↑ Zhu X, Jiang M, Birnbaumer L. Receptor-activated Ca2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative Ca2+ entry. J Biol Chem. 1998 Jan 2;273(1):133-42. PMID:9417057
↑ Hofmann T, Obukhov AG, Schaefer M, Harteneck C, Gudermann T, Schultz G. Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol. Nature. 1999 Jan 21;397(6716):259-63. doi: 10.1038/16711. PMID:9930701 doi:http://dx.doi.org/10.1038/16711
↑ Fan C, Choi W, Sun W, Du J, Lu W. Structure of the human lipid-gated cation channel TRPC3. Elife. 2018 May 4;7. pii: 36852. doi: 10.7554/eLife.36852. PMID:29726814 doi:http://dx.doi.org/10.7554/eLife.36852

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6cud"

@@ Line 1: / Line 1: @@
 ==Structure of the human TRPC3 in a lipid-occupied, closed state==
-<StructureSection load='6cud' size='340' side='right'caption='[[6cud]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+<SX load='6cud' size='340' side='right' viewer='molstar' caption='[[6cud]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6cud]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CUD FirstGlance]. <br>
@@ Line 24: / Line 24: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Human]]
 [[Category: Large Structures]]

6cud

From Proteopedia

Revision as of 20:49, 6 March 2020

Structure of the human TRPC3 in a lipid-occupied, closed state

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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