التفاصيل البيبلوغرافية
العنوان: |
Proton-binding sites of acid-sensing ion channel 1. |
المؤلفون: |
Ishikita, Hiroshi |
المساهمون: |
石北, 央 |
بيانات النشر: |
Public Library of Science |
سنة النشر: |
2011 |
المجموعة: |
Kyoto University Research Information Repository (KURENAI) / 京都大学学術情報リポジトリ |
مصطلحات موضوعية: |
Acid Sensing Ion Channels, Amino Acids, Animals, Binding Sites, Hydrogen-Ion Concentration, Ion Channels/chemistry, Ion Channels/genetics, Ion Channels/metabolism, Ion Channels/physiology, Models, Molecular, Nerve Tissue Proteins/chemistry, Nerve Tissue Proteins/genetics, Nerve Tissue Proteins/metabolism, Nerve Tissue Proteins/physiology, Protein Binding/physiology, Protein Interaction Domains and Motifs/genetics, Protein Interaction Mapping, Protein Multimerization, Protein Structure, Secondary, Protein Subunits, Protons, Sodium Channels/chemistry, Sodium Channels/genetics, Sodium Channels/metabolism, Sodium Channels/physiology |
الوصف: |
Acid-sensing ion channels (ASICs) are proton-gated cation channels that exist throughout the mammalian central and peripheral nervous systems. ASIC1 is the most abundant of all the ASICs and is likely to modulate synaptic transmission. Identifying the proton-binding sites of ASCI1 is required to elucidate its pH-sensing mechanism. By using the crystal structure of ASIC1, the protonation states of each titratable site of ASIC1 were calculated by solving the Poisson-Boltzmann equation under conditions wherein the protonation states of all these sites are simultaneously in equilibrium. Four acidic-acidic residue pairs--Asp238-Asp350, Glu220-Asp408, Glu239-Asp346, and Glu80-Glu417--were found to be highly protonated. In particular, the Glu80-Glu417 pair in the inner pore was completely protonated and possessed 2 H(+), implying its possible importance as a proton-binding site. The pK(a) of Glu239, which forms a pair with a possible pH-sensing site Asp346, differs among each homo-trimer subunit due to the different H-bond pattern of Thr237 in the different protein conformations of the subunits. His74 possessed a pK(a) of ≈6-7. Conservation of His74 in the proton-sensitive ASIC3 that lacks a residue corresponding to Asp346 may suggest its possible pH-sensing role in proton-sensitive ASICs. |
نوع الوثيقة: |
article in journal/newspaper |
وصف الملف: |
application/pdf |
اللغة: |
English |
تدمد: |
1932-6203 |
Relation: |
http://hdl.handle.net/2433/169689; PloS one; e16920 |
الاتاحة: |
http://hdl.handle.net/2433/169689 |
Rights: |
© 2011 Hiroshi Ishikita. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
رقم الانضمام: |
edsbas.475CA92F |
قاعدة البيانات: |
BASE |