1kxi

Structural highlights

Function

3SOF5_NAJAT Non-cytotoxic protein that does not show lytic and hemolytic activities, but can induce aggregation and fusion of sphingomyelin vesicles (PubMed:8182052). It binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with high affinity, and it inhibits osteoclast differentiation and bone resorption in mice, probably due to binding to integrin alpha-V/beta-3 (PubMed:16407244).^{[1] [2] [3] [4]}

Evolutionary Conservation

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

See Also

• Cardiotoxin 3D structures

References

1. ↑ Konshina AG, Volynskii PE, Arsen'ev AS, Efremov RG. [Interaction of cardiotoxin A5 with a membrane: role of conformational heterogeneity and hydrophilic properties] Bioorg Khim. 2003 Nov-Dec;29(6):577-88. PMID:14743531
2. ↑ Wu PL, Lee SC, Chuang CC, Mori S, Akakura N, Wu WG, Takada Y. Non-cytotoxic cobra cardiotoxin A5 binds to alpha(v)beta3 integrin and inhibits bone resorption. Identification of cardiotoxins as non-RGD integrin-binding proteins of the Ly-6 family. J Biol Chem. 2006 Mar 24;281(12):7937-45. Epub 2006 Jan 10. PMID:16407244 doi:http://dx.doi.org/M513035200
3. ↑ Chien KY, Chiang CM, Hseu YC, Vyas AA, Rule GS, Wu W. Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions. J Biol Chem. 1994 May 20;269(20):14473-83. PMID:8182052
4. ↑ Chiang CM, Chien KY, Lin HJ, Lin JF, Yeh HC, Ho PL, Wu WG. Conformational change and inactivation of membrane phospholipid-related activity of cardiotoxin V from Taiwan cobra venom at acidic pH. Biochemistry. 1996 Jul 16;35(28):9167-76. PMID:8703922 doi:http://dx.doi.org/10.1021/bi952823k