[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleA structural basis for amylin receptor phenotype.
Journal, issue, pagesScience, Vol. 375, Issue 6587, Page eabm9609, Year 2022
Publish dateMar 25, 2022
AuthorsJianjun Cao / Matthew J Belousoff / Yi-Lynn Liang / Rachel M Johnson / Tracy M Josephs / Madeleine M Fletcher / Arthur Christopoulos / Debbie L Hay / Radostin Danev / Denise Wootten / Patrick M Sexton /
PubMed AbstractAmylin receptors (AMYRs) are heterodimers of the calcitonin (CT) receptor (CTR) and one of three receptor activity-modifying proteins (RAMPs), AMYR, AMYR, and AMYR. Selective AMYR agonists and dual ...Amylin receptors (AMYRs) are heterodimers of the calcitonin (CT) receptor (CTR) and one of three receptor activity-modifying proteins (RAMPs), AMYR, AMYR, and AMYR. Selective AMYR agonists and dual AMYR/CTR agonists are being developed as obesity treatments; however, the molecular basis for peptide binding and selectivity is unknown. We determined the structure and dynamics of active AMYRs with amylin, AMYR with salmon CT (sCT), AMYR with sCT or human CT (hCT), and CTR with amylin, sCT, or hCT. The conformation of amylin-bound complexes was similar for all AMYRs, constrained by the RAMP, and an ordered midpeptide motif that we call the bypass motif. The CT-bound AMYR complexes were distinct, overlapping the CT-bound CTR complexes. Our findings indicate that activation of AMYRs by CT-based peptides is distinct from their activation by amylin-based peptides. This has important implications for the development of AMYR therapeutics.
External linksScience / PubMed:35324283
MethodsEM (single particle)
Resolution2.2 - 3.3 Å
Structure data

26178

7tyf

EMDB-26178, PDB-7tyf:
Human Amylin1 Receptor in complex with Gs and rat amylin peptide
Method: EM (single particle) / Resolution: 2.2 Å

26179

7tyh

EMDB-26179, PDB-7tyh:
Human Amylin2 Receptor in complex with Gs and human calcitonin peptide
Method: EM (single particle) / Resolution: 3.3 Å

26180

7tyi

EMDB-26180, PDB-7tyi:
Calcitonin Receptor in complex with Gs and rat amylin peptide, CT-like state
Method: EM (single particle) / Resolution: 3.3 Å

26184

7tyl

EMDB-26184, PDB-7tyl:
Calcitonin Receptor in complex with Gs and rat amylin peptide, bypass motif
Method: EM (single particle) / Resolution: 3.3 Å

26188

7tyn

EMDB-26188, PDB-7tyn:
Calcitonin Receptor in complex with Gs and salmon calcitonin peptide
Method: EM (single particle) / Resolution: 2.6 Å

26190

7tyo

EMDB-26190, PDB-7tyo:
Calcitonin receptor in complex with Gs and human calcitonin peptide
Method: EM (single particle) / Resolution: 2.7 Å

26196

7tyw

EMDB-26196, PDB-7tyw:
Human Amylin1 Receptor in complex with Gs and salmon calcitonin peptide
Method: EM (single particle) / Resolution: 3.0 Å

26197

7tyx

EMDB-26197, PDB-7tyx:
Human Amylin2 Receptor in complex with Gs and rat amylin peptide
Method: EM (single particle) / Resolution: 2.55 Å

26199

7tyy

EMDB-26199, PDB-7tyy:
Human Amylin2 Receptor in complex with Gs and salmon calcitonin peptide
Method: EM (single particle) / Resolution: 3.0 Å

26208

7tzf

EMDB-26208, PDB-7tzf:
Human Amylin3 Receptor in complex with Gs and rat amylin peptide
Method: EM (single particle) / Resolution: 2.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-P42:
(2S)-2-{[(1R)-1-hydroxyhexadecyl]oxy}-3-{[(1R)-1-hydroxyoctadecyl]oxy}propyl 2-(trimethylammonio)ethyl phosphate / SPPC, phospholipid*YM

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • lama glama (llama)
  • rattus norvegicus (Norway rat)
  • salmo salar (Atlantic salmon)
KeywordsMEMBRANE PROTEIN / Amylin receptor / GPCR / RAMP / RAMP2 / human calcitonin / calcitonin / CT-like / Amylin / bypass motif / calcitonin receptor / salmon calcitonin / RAMP1 / RAMP3 / rat amylin

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more