Crystal structure of CapZ bound to the CPI and CSI uncapping motifs from CARMILCrystal structure of CapZ bound to the CPI and CSI uncapping motifs from CARMIL

Structural highlights

3lk3 is a 3 chain structure with sequence from Gallus gallus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:CAPZA1 (Gallus gallus), CAPZB (Gallus gallus), CARMIL, LRRC16, LRRC16A (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[CAZA1_CHICK] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. CapZ may mediate the attachment of the barbed ends of actin filaments to the Z-line. [LR16A_HUMAN] Binds CAPZA2 with high affinity and significantly decreases CAPZA2 affinity for actin barbed ends. Increases the rate of elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Rapidly uncaps barbed ends capped by CAPZA2 and enhances barbed-end actin polymerization (By similarity).[1] [CAPZB_CHICK] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the regulation of cell morphology and cytoskeletal organization.

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Yang C, Pring M, Wear MA, Huang M, Cooper JA, Svitkina TM, Zigmond SH. Mammalian CARMIL inhibits actin filament capping by capping protein. Dev Cell. 2005 Aug;9(2):209-21. PMID:16054028 doi:http://dx.doi.org/10.1016/j.devcel.2005.06.008

3lk3, resolution 2.68Å

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OCA