3CX2

Crystal structure of the C1 domain of cardiac isoform of myosin binding protein-C at 1.3A

Summary for 3CX2

• Entry DOI: 10.2210/pdb3cx2/pdb
• Related: 2V6H
• Descriptor: Myosin-binding protein C, cardiac-type (2 entities in total)
• Functional Keywords: myosin-binding protein; protonation states, actin-binding, cardiomyopathy, cell adhesion, disease mutation, immunoglobulin domain, muscle protein, phosphoprotein, polymorphism, thick filament, contractile protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 12049.61

Authors

Fisher, S.J.,Helliwell, J.R.,Khurshid, S.,Govada, L.,Redwood, C.,Squire, J.M.,Chayen, N.E. (deposition date: 2008-04-23, release date: 2008-07-01, Last modification date: 2023-08-30)

Primary citation

Fisher, S.J.,Helliwell, J.R.,Khurshid, S.,Govada, L.,Redwood, C.,Squire, J.M.,Chayen, N.E.
An investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C
Acta Crystallogr.,Sect.D, 64:658-664, 2008

PubMed Abstract: Myosin-binding protein C (MyBP-C) is a myofibril-associated protein found in cardiac and skeletal muscle. The cardiac isoform (cMyBP-C) is subject to reversible phosphorylation and the surface-charge state of the protein is of keen interest with regard to understanding the inter-protein interactions that are implicated in its function. Diffraction data from the C1 domain of cMyBP-C were extended to 1.30 A resolution, where the of the diffraction data crosses 2.0, using intense synchrotron radiation. The protonation-state determinations were not above 2sigma (the best was 1.81sigma) and therefore an extrapolation is given, based on 100% data completeness and the average DPI, that a 3sigma determination could be possible if X-ray data could be measured to 1.02 A resolution. This might be possible via improved crystallization or multiple sample evaluation, e.g. using robotics or a yet more intense/collimated X-ray beam or combinations thereof. An alternative would be neutron protein crystallography at 2 A resolution, where it is estimated that for the unit-cell volume of the cMyBP-C C1 domain crystal a crystal volume of 0.10 mm3 would be needed with fully deuterated protein on LADI III. These efforts would optimally be combined in a joint X-ray and neutron model refinement.

PubMed: 18560154
DOI: 10.1107/S0907444908008792

Experimental method

X-RAY DIFFRACTION (1.3 Å)