2N9Y

Structure of the Integrin alphaIIb-beta3(A711P) Transmembrane Complex

Summary for 2N9Y

• Entry DOI: 10.2210/pdb2n9y/pdb
• Related: 2K9J
• NMR Information: BMRB: 25920
• Descriptor: Integrin alpha-IIb, Integrin beta-3 (2 entities in total)
• Functional Keywords: transmembrane complex, integrin receptor, cell adhesion, helix kink, membrane protein-cell adhesion complex, membrane protein/cell adhesion
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P08514; Cell membrane ; Single- pass type I membrane protein : P05106
• Total number of polymer chains: 2
• Total formula weight: 9528.75

Authors

Schmidt, T.,Situ, A.J.,Ulmer, T.S. (deposition date: 2015-12-14, release date: 2016-08-03, Last modification date: 2024-11-06)

Primary citation

Schmidt, T.,Situ, A.J.,Ulmer, T.S.
Structural and thermodynamic basis of proline-induced transmembrane complex stabilization.
Sci Rep, 6:29809-29809, 2016

PubMed Abstract: In membrane proteins, proline-mediated helix kinks are indispensable for the tight packing of transmembrane (TM) helices. However, kinks invariably affect numerous interhelical interactions, questioning the acceptance of proline substitutions and evolutionary origin of kinks. Here, we present the structural and thermodynamic basis of proline-induced integrin αIIbβ3 TM complex stabilization to understand the introduction of proline kinks in membrane proteins. In phospholipid bicelles, the A711P substitution in the center of the β3 TM helix changes the direction of adjacent helix segments to form a 35 ± 2° angle and predominantly repacks the segment in the inner membrane leaflet due to a swivel movement. This swivel repacks hydrophobic and electrostatic interhelical contacts within intracellular lipids, resulting in an overall TM complex stabilization of -0.82 ± 0.01 kcal/mol. Thus, proline substitutions can directly stabilize membrane proteins and such substitutions are proposed to follow the structural template of integrin αIIbβ3(A711P).

PubMed: 27436065
DOI: 10.1038/srep29809

Experimental method

SOLUTION NMR