Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
Reported here is the 2.3 A resolution crystal structure of spruce budworm (Choristoneura fumiferana) antifreeze protein (CfAFP), solved by single anomalous scattering. The structure reveals an extremely regular left-handed beta-helical platform consisting of 15-amino acid loops with a repetitive Thr-X-Thr motif displayed on one of the helix's three faces. This motif results in a two-dimensional array of threonine residues in an identical orientation to those in the nonhomologous, right-handed beta-helical beetle AFP from Tenebrio molitor (TmAFP). The CfAFP structure led us to reevaluate our ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity. This general mechanism is applicable to both fish and insect AFPs.
Crystal structure of beta-helical antifreeze protein points to a general ice binding model.,Leinala EK, Davies PL, Jia Z Structure. 2002 May;10(5):619-27. PMID:12015145[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Leinala EK, Davies PL, Jia Z. Crystal structure of beta-helical antifreeze protein points to a general ice binding model. Structure. 2002 May;10(5):619-27. PMID:12015145
