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4LZX

Complex of IQCG and Ca2+-free CaM

Summary for 4LZX
Entry DOI10.2210/pdb4lzx/pdb
Related4M1L
DescriptorCalmodulin, IQ domain-containing protein G, SULFATE ION, ... (4 entities in total)
Functional Keywordsprotein complex, iq domain; ef hand domains, calcium signalling, metal binding protein
Biological sourceHomo sapiens (human)
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Cellular locationCytoplasm, cytoskeleton, spindle : P62158
Total number of polymer chains2
Total formula weight21408.90
Authors
Liang, W.X.,Chen, L.T.,Chen, Z.,Chen, S.J.,Chen, S. (deposition date: 2013-08-01, release date: 2014-05-07, Last modification date: 2024-03-20)
Primary citationChen, L.T.,Liang, W.X.,Chen, S.,Li, R.K.,Tan, J.L.,Xu, P.F.,Luo, L.F.,Wang, L.,Yu, S.H.,Meng, G.,Li, K.K.,Liu, T.X.,Chen, Z.,Chen, S.J.
Functional and molecular features of the calmodulin-interacting protein IQCG required for haematopoiesis in zebrafish
Nat Commun, 5:3811-3811, 2014
Cited by
PubMed Abstract: We previously reported a fusion protein NUP98-IQCG in an acute leukaemia, which functions as an aberrant regulator of transcriptional expression, yet the structure and function of IQCG have not been characterized. Here we use zebrafish to investigate the role of iqcg in haematopoietic development, and find that the numbers of haematopoietic stem cells and multilineage-differentiated cells are reduced in iqcg-deficient embryos. Mechanistically, IQCG binds to calmodulin (CaM) and acts as a molecule upstream of CaM-dependent kinase IV (CaMKIV). Crystal structures of complexes between CaM and IQ domain of IQCG reveal dual CaM-binding footprints in this motif, and provide a structural basis for a higher CaM-IQCG affinity when deprived of calcium. The results collectively allow us to understand IQCG-mediated calcium signalling in haematopoiesis, and propose a model in which IQCG stores CaM at low cytoplasmic calcium concentrations, and releases CaM to activate CaMKIV when calcium level rises.
PubMed: 24787902
DOI: 10.1038/ncomms4811
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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