3zym: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Structure of CALM (PICALM) in complex with VAMP8== | ==Structure of CALM (PICALM) in complex with VAMP8== | ||
<StructureSection load='3zym' size='340' side='right' caption='[[3zym]], [[Resolution|resolution]] 2.03Å' scene=''> | <StructureSection load='3zym' size='340' side='right'caption='[[3zym]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zym]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYM FirstGlance]. <br> | <table><tr><td colspan='2'>[[3zym]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYM FirstGlance]. <br> | ||
Line 23: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Graham, S C]] | [[Category: Graham, S C]] |
Revision as of 15:29, 13 March 2019
Structure of CALM (PICALM) in complex with VAMP8Structure of CALM (PICALM) in complex with VAMP8
Structural highlights
Function[PICA_RAT] Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction (By similarity).[UniProtKB:Q13492] Publication Abstract from PubMedSNAREs provide a large part of the specificity and energy needed for membrane fusion and, to do so, must be localized to their correct membranes. Here, we show that the R-SNAREs VAMP8, VAMP3, and VAMP2, which cycle between the plasma membrane and endosomes, bind directly to the ubiquitously expressed, PtdIns4,5P(2)-binding, endocytic clathrin adaptor CALM/PICALM. X-ray crystallography shows that the N-terminal halves of their SNARE motifs bind the CALM(ANTH) domain as helices in a manner that mimics SNARE complex formation. Mutation of residues in the CALM:SNARE interface inhibits binding in vitro and prevents R-SNARE endocytosis in vivo. Thus, CALM:R-SNARE interactions ensure that R-SNAREs, required for the fusion of endocytic clathrin-coated vesicles with endosomes and also for subsequent postendosomal trafficking, are sorted into endocytic vesicles. CALM's role in directing the endocytosis of small R-SNAREs may provide insight into the association of CALM/PICALM mutations with growth retardation, cognitive defects, and Alzheimer's disease. The Molecular Basis for the Endocytosis of Small R-SNAREs by the Clathrin Adaptor CALM.,Miller SE, Sahlender DA, Graham SC, Honing S, Robinson MS, Peden AA, Owen DJ Cell. 2011 Nov 23;147(5):1118-31. PMID:22118466[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|