2X43

STRUCTURAL BASIS OF MOLECULAR RECOGNITION BY SHERP AT MEMBRANE SURFACES

2X43 の概要

• エントリーDOI: 10.2210/pdb2x43/pdb
• 分子名称: SHERP (1 entity in total)
• 機能のキーワード: membrane protein
• 由来する生物種: LEISHMANIA MAJOR
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7267.88

構造登録者

Moore, B.,Miles, A.J.,Guerra, C.G.,Simpson, P.,Iwata, M.,Wallace, B.A.,Matthews, S.J.,Smith, D.F.,Brown, K.A. (登録日: 2010-02-09, 公開日: 2010-11-24, 最終更新日: 2024-05-15)

主引用文献

Moore, B.,Miles, A.J.,Guerra, C.G.,Simpson, P.,Iwata, M.,Wallace, B.A.,Matthews, S.J.,Smith, D.F.,Brown, K.A.
Structural Basis of Moelcular Recognition by the Leishmania Small Hydrophilic Endoplasmic Reticulum-Associated Protein, Sherp, at Membrane Surfaces
J.Biol.Chem., 286:9246-, 2011

PubMed Abstract: The 57-residue small hydrophilic endoplasmic reticulum-associated protein (SHERP) shows highly specific, stage-regulated expression in the non-replicative vector-transmitted stages of the kinetoplastid parasite, Leishmania major, the causative agent of human cutaneous leishmaniasis. Previous studies have demonstrated that SHERP localizes as a peripheral membrane protein on the cytosolic face of the endoplasmic reticulum and on outer mitochondrial membranes, whereas its high copy number suggests a critical function in vivo. However, the absence of defined domains or identifiable orthologues, together with lack of a clear phenotype in transgenic parasites lacking SHERP, has limited functional understanding of this protein. Here, we use a combination of biophysical and biochemical methods to demonstrate that SHERP can be induced to adopt a globular fold in the presence of anionic lipids or SDS. Cross-linking and binding studies suggest that SHERP has the potential to form a complex with the vacuolar type H(+)-ATPase. Taken together, these results suggest that SHERP may function in modulating cellular processes related to membrane organization and/or acidification during vector transmission of infective Leishmania.

PubMed: 21106528
DOI: 10.1074/JBC.M110.130427

実験手法

SOLUTION NMR