4BL4

Further structural insights into the binding of complement factor H by complement regulator acquiring surface protein 1, CspA (BbCRASP-1), of Borrelia burgdorferi.

「4ATR」から置き換えられました

4BL4 の概要

• エントリーDOI: 10.2210/pdb4bl4/pdb
• 分子名称: COMPLEMENT REGULATOR-ACQUIRING SURFACE PROTEIN 1 (CRASP-1) (1 entity in total)
• 機能のキーワード: protein binding
• 由来する生物種: BORRELIA BURGDORFERI (LYME DISEASE SPIROCHETE)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 85914.37

構造登録者

Caesar, J.J.E.,Wallich, R.,Kraiczy, P.,Zipfel, P.F.,Lea, S.M. (登録日: 2013-05-01, 公開日: 2013-06-05, 最終更新日: 2023-12-20)

主引用文献

Caesar, J.J.E.,Wallich, R.,Kraiczy, P.,Zipfel, P.F.,Lea, S.M.
Further Structural Insights Into the Binding of Complement Factor H by Complement Regulator-Acquiring Surface Protein 1 (CspA) of Borrelia Burgdorferi.
Acta Crystallogr.,Sect.F, 69:629-, 2013

PubMed Abstract: Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators.

PubMed: 23722839
DOI: 10.1107/S1744309113012748

実験手法

X-RAY DIFFRACTION (4.06 Å)