2LX4
NMR solution structure of peptide a2N(1-17) from Mus musculus V-ATPase
Summary for 2LX4
Entry DOI | 10.2210/pdb2lx4/pdb |
NMR Information | BMRB: 18658 |
Descriptor | V-type proton ATPase 116 kDa subunit a isoform 2 (1 entity in total) |
Functional Keywords | v-atpase, subunit a, alpha helix, ph sensor, sec7 binding motif, proton transport |
Biological source | Mus musculus (mouse) |
Cellular location | Cell membrane; Multi-pass membrane protein: P15920 |
Total number of polymer chains | 1 |
Total formula weight | 1934.33 |
Authors | Dip, P.,Gruber, G.,Marshansky, V. (deposition date: 2012-08-14, release date: 2013-01-09, Last modification date: 2024-05-01) |
Primary citation | Hosokawa, H.,Dip, P.V.,Merkulova, M.,Bakulina, A.,Zhuang, Z.,Khatri, A.,Jian, X.,Keating, S.M.,Bueler, S.A.,Rubinstein, J.L.,Randazzo, P.A.,Ausiello, D.A.,Gruber, G.,Marshansky, V. The N Termini of a-Subunit Isoforms Are Involved in Signaling between Vacuolar H+-ATPase (V-ATPase) and Cytohesin-2. J.Biol.Chem., 288:5896-5913, 2013 Cited by PubMed: 23288846DOI: 10.1074/jbc.M112.409169 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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