1GQM

The structure of S100A12 in a hexameric form and its proposed role in receptor signalling

1GQM の概要

• エントリーDOI: 10.2210/pdb1gqm/pdb
• 関連するPDBエントリー: 1E8A
• 分子名称: CALGRANULIN C, CALCIUM ION (3 entities in total)
• 機能のキーワード: antimicrobial protein, s100a12, s100 protein family, ef-hand, calcium binding
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 126972.82

構造登録者

Moroz, O.V.,Antson, A.A.,Dodson, E.G.,Burrel, H.J.,Grist, S.J.,Lloyd, R.M.,Maitland, N.J.,Dodson, G.G.,Wilson, K.S.,Lukanidin, E.,Bronstein, I.B. (登録日: 2001-11-26, 公開日: 2002-02-28, 最終更新日: 2023-12-13)

主引用文献

Moroz, O.V.,Antson, A.A.,Dodson, E.J.,Burrell, H.J.,Grist, S.J.,Lloyd, R.M.,Maitland, N.J.,Dodson, G.G.,Wilson, K.S.,Lukanidin, E.,Bronstein, I.B.
The Structure of S100A12 in a Hexameric Form and its Proposed Role in Receptor Signalling
Acta Crystallogr.,Sect.D, 58:407-, 2002

PubMed Abstract: S100A12 is a member of the S100 subfamily of EF-hand calcium-binding proteins; it has been shown to be one of the ligands of the 'receptor for advanced glycation end products' (RAGE) that belongs to the immunoglobulin superfamily and is involved in diabetes, Alzheimer's disease, inflammation and tumour invasion. The structure of the dimeric form of native S100A12 from human granulocytes in the presence of calcium in space group R3 has previously been reported. Here, the structure of a second crystal form in space group P2(1) (unit-cell parameters a = 53.9, b = 100.5, c = 112.7A, beta = 94.6 degrees) solved at 2.7A resolution by molecular replacement using the R3 structure as a search model is reported. Like most S100 proteins, S100A12 is a dimer. However, in the P2(1) crystal form dimers of S100A12 are arranged in a spherical hexameric assembly with an external diameter of about 55 A stabilized by calcium ions bound between adjacent dimers. The putative target-binding sites of S100A12 are located at the outer surface of the hexamer, making it possible for the hexamer to bind several targets. It is proposed that the S100A12 hexameric assembly might interact with three extracellular domains of the receptor, bringing them together into large trimeric assemblies.

PubMed: 11856825
DOI: 10.1107/S0907444901021278

実験手法

X-RAY DIFFRACTION (2.7 Å)