Tu banner alternativo

Calx-beta motif

In today's article we will talk about Calx-beta motif, a topic that has become increasingly relevant in recent years. Calx-beta motif has become a point of interest for many people, whether due to its impact on society, its historical relevance or its influence on popular culture. Throughout this article we will explore different aspects related to Calx-beta motif, from its origin and evolution, to its current and future projection. We will discover its importance in people's lives and how it has been setting standards in various areas. Without a doubt, Calx-beta motif is a topic that generates great interest and from which we can learn a lot.

Tu banner alternativo
Calx-beta
first ca2+ binding domain of the na,ca-exchanger (ncx1)
Identifiers
SymbolCalx-beta
PfamPF03160
InterProIPR003644
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the calx-beta motif is a protein motif which is present as a tandem repeat in the cytoplasmic domains of Calx sodium-calcium exchangers, which are used to expel calcium from cells. This motif overlaps domains used for calcium binding and regulation. The calx-beta motif is also present in the cytoplasmic tail of mammalian integrin-beta4, which mediates the bi-directional transfer of signals across the plasma membrane, as well as in some cyanobacterial proteins. This motif contains a series of beta-strands and turns that form a self-contained beta-sheet.[1][2]

References

  1. ^ Schwarz EM, Benzer S (September 1997). "Calx, a Na-Ca exchanger gene of Drosophila melanogaster". Proceedings of the National Academy of Sciences of the United States of America. 94 (19): 10249–54. Bibcode:1997PNAS...9410249S. doi:10.1073/pnas.94.19.10249. PMC 23348. PMID 9294196.
  2. ^ Schwarz E, Benzer S (July 1999). "The recently reported NIbeta domain is already known as the Calx-beta motif". Trends in Biochemical Sciences. 24 (7): 260. doi:10.1016/S0968-0004(99)01422-X. PMID 10390612.
This article incorporates text from the public domain Pfam and InterPro: IPR003644