2D46

Solution Structure of the Human Beta4a-A Domain

Summary for 2D46

• Entry DOI: 10.2210/pdb2d46/pdb
• Descriptor: calcium channel, voltage-dependent, beta 4 subunit isoform a (1 entity in total)
• Functional Keywords: ca2+ channel, beta4a subunit, alternative spliving, membrane-associated guanylate-kinase, protein structure, metal transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 6877.30

Authors

Vendel, A.C.,Rithner, C.D.,Lyons, B.A.,Horne, W.A. (deposition date: 2005-10-10, release date: 2005-10-25, Last modification date: 2024-05-29)

Primary citation

Vendel, A.C.,Rithner, C.D.,Lyons, B.A.,Horne, W.A.
Solution structure of the N-terminal A domain of the human voltage-gated Ca2+channel beta4a subunit
Protein Sci., 15:378-383, 2006

PubMed Abstract: Ca2+ channel beta subunits regulate trafficking and gating (opening and closing) of voltage-dependent Ca2+ channel alpha1 subunits. Based on primary sequence comparisons, they are thought to be modular structures composed of five domains (A-E) that are related to the large family of membrane associated guanylate-kinase (MAGUK) proteins. The crystal structures of the beta subunit core, B-D, domains have recently been reported; however, very little is known about the structures of the A and E domains. The N-terminal A domain is a hypervariable region that differs among the four subtypes of Ca2+ channel beta subunits (beta1-beta4). Furthermore, this domain undergoes alternative splicing to create multiple N-terminal structures within a given gene class that have distinct effects on gating. We have solved the solution structure of the A domain of the human beta4a subunit, a splice variant that we have shown previously to have alpha1 subunit subtype-specific effects on Ca2+ channel trafficking and gating.

PubMed: 16385006
DOI: 10.1110/ps.051894506

Experimental method

SOLUTION NMR