Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2013 Jul;142(1):37–60. doi: 10.1085/jgp.201210933

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2013 Morales et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

PMC Copyright notice

Figure 2. — Structural analysis of the CaM–CaMBD2 interactions. (A and B) SASA was computed for each residue of CaMBD2B (K360-K373) or CaMBD2A (L344-Q353) for either a single KCa3.1 subunit with no CaM (open boxes) or in the presence of a second subunit with no CaM (filled boxes). Calculations were based on the structural model presented in Fig. 1. A strong decrease in SASA was obtained for E363 and S367, indicating an important contribution to the intersubunit interface. Identical calculations performed for residues in CaMBD2A identified L345 and N349 as contributing to the intersubunit interface. (C and D) Variations in SASA caused by the addition of CaM to the KCa3.1 subunit–subunit complex. A strong decrease in SASA caused by CaM was obtained for Q364, M368, V369, and S372 in agreement with those residues lining the CaMBD2B–CaM N-lobe interface. The most important variation was seen with M368, which is projecting inside the CaM N-lobe core. In contrast, SASA computed for R362 and E363 were not significantly affected by the addition of CaM, in accordance with R362 and E363 not contributing to the CaMBD2B–CaM N-lobe interface. Collectively, R362 appeared as the most solvent accessible residue, with no contribution to either the intersubunit or CaMBD2B–CaM N-lobe interfaces. Results obtained for the CaMBD2A support a strong decrease in SASA caused by CaM for I348, N349, and F351, an indication that these residues are located at the CaMBD2A–CaM interface. Residue R352 was found to be highly solvent accessible, with 50% of its surface in contact with CaM.