1lin: Difference between revisions
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==CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)== | ==CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)== | ||
<StructureSection load='1lin' size='340' side='right' caption='[[1lin]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1lin' size='340' side='right'caption='[[1lin]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lin]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LIN FirstGlance]. <br> | <table><tr><td colspan='2'>[[1lin]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LIN FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Calmodulin|Calmodulin]] | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Delbaere, L T.J]] | [[Category: Delbaere, L T.J]] | ||
[[Category: Hickie, R A]] | [[Category: Hickie, R A]] |
Revision as of 20:42, 22 January 2020
CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)
Structural highlights
Function[CALM_BOVIN] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHere we show that, as a consequence of binding the drug trifluoperazine, a major conformational movement occurs in Ca(2+)-calmodulin (CaM). The tertiary structure changes from an elongated dumb-bell, with exposed hydrophobic surfaces, to a compact globular form which can no longer interact with its target enzymes. It is likely that inactivation of Ca(2+)-CaM by trifluoperazine is due to this major tertiary-structural alteration in Ca(2+)-CaM, which is initiated and stabilized by drug binding. This conformational change is similar to that which occurs on the binding of Ca(2+)-CaM to target peptides. Two hydrophobic binding pockets, created by amino acid residues adjacent to Ca(2+)-coordinating residues, form the key recognition sites on Ca(2+)-CaM for both inhibitors and target enzymes. Trifluoperazine-induced conformational change in Ca(2+)-calmodulin.,Vandonselaar M, Hickie RA, Quail JW, Delbaere LT Nat Struct Biol. 1994 Nov;1(11):795-801. PMID:7634090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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