1N42

Crystal Structure of Annexin V R149E Mutant

1N42 の概要

• エントリーDOI: 10.2210/pdb1n42/pdb
• 分子名称: Annexin V, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: calcium, phospholipid, membrane binding protein, lipid binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36248.96

構造登録者

Mo, Y.D.,Campos, B.,Mealy, T.R.,Commodore, L.,Head, J.F.,Dedman, J.R.,Seaton, B.A. (登録日: 2002-10-30, 公開日: 2003-02-04, 最終更新日: 2024-02-14)

主引用文献

Mo, Y.D.,Campos, B.,Mealy, T.R.,Commodore, L.,Head, J.F.,Dedman, J.R.,Seaton, B.A.
Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces
J.Biol.Chem., 278:2437-2443, 2003

PubMed Abstract: Annexin V is an abundant eukaryotic protein that binds phospholipid membranes in a Ca(2+)-dependent manner. In the present studies, site-directed mutagenesis was combined with x-ray crystallography and solution liposome binding assays to probe the functional role of a cluster of interfacial basic residues in annexin V. Four mutants were investigated: R23E, K27E, R61E, and R149E. All four mutants exhibited a significant reduction in adsorption to phospholipid membranes relative to the wild-type protein, and the R23E mutation was the most deleterious. Crystal structures of wild-type and mutant proteins were similar except for local changes in salt bridges involving basic cluster residues. The combined data indicate that Arg(23) is a major determinant for interfacial phospholipid binding and participates in an intermolecular salt bridge that is key for trimer formation on the membrane surface. Together, crystallographic and solution data provide evidence that the interfacial basic cluster is a locus where trimerization is synergistically coupled to membrane phospholipid binding.

PubMed: 12401794
DOI: 10.1074/jbc.M210286200

実験手法

X-RAY DIFFRACTION (2.1 Å)