4HTI

Crystallographic structure of the membrane-proximal ectodomain of the human receptor-type protein-tyrosine phosphatase phogrin

4HTI の概要

• エントリーDOI: 10.2210/pdb4hti/pdb
• 分子名称: Receptor-type tyrosine-protein phosphatase N2 (2 entities in total)
• 機能のキーワード: phogrin, ia-2beta, protein-tyrosine phosphatase, transmembrane protein, diabetes, autoimmunity, glycoprotein, receptor, hydrolase, ferredoxin-like fold
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle membrane ; Single-pass type I membrane protein . IA-2beta60: Cytoplasmic vesicle, secretory vesicle membrane : Q92932
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10826.07

構造登録者

Noguera, M.E.,Jakoncic, J.,Poskus, E.,Ermacora, M.R. (登録日: 2012-11-01, 公開日: 2012-11-28, 最終更新日: 2023-09-20)

主引用文献

Noguera, M.E.,Primo, M.E.,Jakoncic, J.,Poskus, E.,Solimena, M.,Ermacora, M.R.
X-ray structure of the mature ectodomain of phogrin.
J.Struct.Funct.Genom., 16:1-9, 2015

PubMed Abstract: Phogrin/IA-2β and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet β-cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and β-cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure-function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel β-strands packed against two α-helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes.

PubMed: 25421040
DOI: 10.1007/s10969-014-9191-0

実験手法

X-RAY DIFFRACTION (1.954 Å)