3TQ7

EB1c/EB3c heterodimer in complex with the CAP-Gly domain of P150glued

Summary for 3TQ7

• Entry DOI: 10.2210/pdb3tq7/pdb
• Related: 1WU9 2HKQ
• Descriptor: Microtubule-associated protein RP/EB family member 1, Microtubule-associated protein RP/EB family member 3, Dynactin subunit 1, ... (4 entities in total)
• Functional Keywords: cap-gly domain, protein-protein interaction, microtubule binding, cytoskeleton, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton: Q15691 Q9UPY8; Cytoplasm: Q14203
• Total number of polymer chains: 4
• Total formula weight: 34149.08

Authors

De Groot, C.O.,Scharer, M.A.,Capitani, G.,Steinmetz, M.O. (deposition date: 2011-09-09, release date: 2012-01-25, Last modification date: 2023-09-13)

Primary citation

Bjelic, S.,De Groot, C.O.,Scharer, M.A.,Jaussi, R.,Bargsten, K.,Salzmann, M.,Frey, D.,Capitani, G.,Kammerer, R.A.,Steinmetz, M.O.
Interaction of mammalian end binding proteins with CAP-Gly domains of CLIP-170 and p150(glued).
J.Struct.Biol., 177:160-167, 2012

PubMed Abstract: End binding proteins (EBs) track growing microtubule ends and play a master role in organizing dynamic protein networks. Mammalian cells express up to three different EBs (EB1, EB2, and EB3). Besides forming homodimers, EB1 and EB3 also assemble into heterodimers. One group of EB-binding partners encompasses proteins that harbor CAP-Gly domains. The binding properties of the different EBs towards CAP-Gly proteins have not been systematically investigated. This information is, however, important to compare and contrast functional differences. Here we analyzed the interactions between CLIP-170 and p150(glued) CAP-Gly domains with the three EB homodimers and the EB1-EB3 heterodimer. Using isothermal titration calorimetry we observed that some EBs bind to the individual CAP-Gly domains with similar affinities while others interact with their targets with pronounced differences. We further found that the two types of CAP-Gly domains use alternative mechanisms to target the C-terminal domains of EBs. We succeeded to solve the crystal structure of a complex composed of a heterodimer of EB1 and EB3 C-termini together with the CAP-Gly domain of p150(glued). Together, our results provide mechanistic insights into the interaction properties of EBs and offer a molecular framework for the systematic investigation of their functional differences in cells.

PubMed: 22119847
DOI: 10.1016/j.jsb.2011.11.010

Experimental method

X-RAY DIFFRACTION (2.3 Å)