1T3S

Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core

Summary for 1T3S

• Entry DOI: 10.2210/pdb1t3s/pdb
• Related: 1T3L
• Descriptor: Dihydropyridine-sensitive L-type, calcium channel beta-2 subunit, MERCURY (II) ION (3 entities in total)
• Functional Keywords: sh3 domain, guanylate kinase domain, transport protein
• Biological source: Oryctolagus cuniculus (rabbit); More
• Cellular location: Cell membrane, sarcolemma ; Peripheral membrane protein ; Cytoplasmic side : P54288
• Total number of polymer chains: 1
• Total formula weight: 38541.54

Authors

Opatowsky, Y.,Chen, C.-C.,Campbell, K.P.,Hirsch, J.A. (deposition date: 2004-04-27, release date: 2004-05-25, Last modification date: 2024-04-03)

Primary citation

Opatowsky, Y.,Chen, C.C.,Campbell, K.P.,Hirsch, J.A.
Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha 1 interaction domain.
Neuron, 42:387-399, 2004

PubMed Abstract: Voltage-dependent calcium channels (VDCC) are multiprotein assemblies that regulate the entry of extracellular calcium into electrically excitable cells and serve as signal transduction centers. The alpha1 subunit forms the membrane pore while the intracellular beta subunit is responsible for trafficking of the channel to the plasma membrane and modulation of its electrophysiological properties. Crystallographic analyses of a beta subunit functional core alone and in complex with a alpha1 interaction domain (AID) peptide, the primary binding site of beta to the alpha1 subunit, reveal that beta represents a novel member of the MAGUK protein family. The findings illustrate how the guanylate kinase fold has been fashioned into a protein-protein interaction module by alteration of one of its substrate sites. Combined results indicate that the AID peptide undergoes a helical transition in binding to beta. We outline the mechanistic implications for understanding the beta subunit's broad regulatory role of the VDCC, particularly via the AID.

PubMed: 15134636
DOI: 10.1093/hmg/ddh162

Experimental method

X-RAY DIFFRACTION (2.3 Å)