2v01: Difference between revisions
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==Recombinant vertebrate calmodulin complexed with Pb== | ==Recombinant vertebrate calmodulin complexed with Pb== | ||
<StructureSection load='2v01' size='340' side='right' caption='[[2v01]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='2v01' size='340' side='right'caption='[[2v01]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v01]] is a 1 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=2V01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V01 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2v01]] is a 1 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=2V01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V01 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: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Kursula, P]] | [[Category: Kursula, P]] | ||
[[Category: Majava, V]] | [[Category: Majava, V]] | ||
Revision as of 17:03, 18 December 2019
Recombinant vertebrate calmodulin complexed with PbRecombinant vertebrate calmodulin complexed with Pb
Structural highlights
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 PubMedCalmodulin is a calcium sensor that is also capable of binding and being activated by other metal ions. Of specific interest in this respect is lead, which is known to be neurotoxic and to have a very high affinity towards calmodulin. Crystal structures of human calmodulin complexed with lead and barium ions have been solved. The results will help in understanding the activation mechanisms of calmodulin by different heavy metals and will provide a detailed view of a putative target for lead neurotoxicity in humans. A structural insight into lead neurotoxicity and calmodulin activation by heavy metals.,Kursula P, Majava V Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):653-6. Epub 2007 Jul 28. PMID:17671360[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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