1VYT

beta3 subunit complexed with aid

Summary for 1VYT

• Entry DOI: 10.2210/pdb1vyt/pdb
• Related: 1VYU 1VYV
• Descriptor: CALCIUM CHANNEL BETA-3 SUBUNIT, VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL ALPHA-1C SUBUNIT (3 entities in total)
• Functional Keywords: transport protein, ion transport-complex, calcium channel beta subunit, aid doamin, ion transport, ionic channel, voltage-gated channel, sh3 domain
• Biological source: RATTUS NORVEGICUS (RAT); More
• Cellular location: Membrane; Multi-pass membrane protein: P22002
• Total number of polymer chains: 4
• Total formula weight: 85152.56

Authors

Chen, Y.-H.,Li, M.-H.,Zhang, Y.,He, L.-L.,Yamada, Y.,Fitzmaurice, A.,Yang, S.,Zhang, H.,Tong, L.,Yang, J. (deposition date: 2004-05-07, release date: 2004-06-15, Last modification date: 2024-10-16)

Primary citation

Chen, Y.-H.,Li, M.-H.,Zhang, Y.,He, L.-L.,Yamada, Y.,Fitzmaurice, A.,Shen, Y.,Zhang, H.,Tong, L.,Yang, J.
Structural Basis of the Alpha(1)-Beta Subunit Interaction of Voltage-Gated Ca(2+) Channels
Nature, 429:675-, 2004

PubMed Abstract: High-voltage-activated Ca2+ channels are essential for diverse biological processes. They are composed of four or five subunits, including alpha1, alpha2-delta, beta and gamma (ref. 1). Their expression and function are critically dependent on the beta-subunit, which transports alpha1 to the surface membrane and regulates diverse channel properties. It is believed that the beta-subunit interacts with alpha1 primarily through the beta-interaction domain (BID), which binds directly to the alpha-interaction domain (AID) of alpha1; however, the molecular mechanism of the alpha1-beta interaction is largely unclear. Here we report the crystal structures of the conserved core region of beta3, alone and in complex with AID, and of beta4 alone. The structures show that the beta-subunit core contains two interacting domains: a Src homology 3 (SH3) domain and a guanylate kinase (GK) domain. The AID binds to a hydrophobic groove in the GK domain through extensive interactions, conferring extremely high affinity between alpha1 and beta-subunits. The BID is essential both for the structural integrity of and for bridging the SH3 and GK domains, but it does not participate directly in binding alpha1. The presence of multiple protein-interacting modules in the beta-subunit opens a new dimension to its function as a multi-functional protein.

PubMed: 15170217
DOI: 10.1038/NATURE02641

Experimental method

X-RAY DIFFRACTION (2.6 Å)