O60894: Receptor activity-modifying protein 1 (RAMP1)

Receptor activity-modifying protein 1 (RAMP1) is a 148-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60894.

Gene
RAMP1
Organism
Homo sapiens
Length
148 residues
Mean pLDDT
89.8
Model
AF-O60894-F1 v6
Model created
1 Aug 2025
PDB structures
25

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate74%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Accessory protein that interacts with and modulates the function of G protein-coupled receptors including calcitonin gene-related peptide type 1 receptor (CALCRL) and calcitonin receptor (CALCR) (PubMed:33602864, PubMed:9620797, PubMed:35324283, PubMed:38603770). Required for the transport of CALCRL to the plasma membrane (PubMed:9620797). Together with CALCRL, form the receptor complex for the calcitonin gene-related peptides CGRP1/CALCA and CGRP2/CALCB (PubMed:33602864, PubMed:9620797). Together with CALCR, form the AMYR1 receptor complex for amylin/IAPP and CGRP1/CALCA (PubMed:35324283, PubMed:38603770)

Subunit structure

Heterodimer of CALCRL and RAMP1; the interaction induces allosteric modulation of CALCRL function and CGRP1/CALCA and CGRP2/CALCB ligand specificity (PubMed:18725456, PubMed:20826335, PubMed:33602864). Heterodimer of CALCR and RAMP1; interaction forms the AMYR1 receptor complex for amylin/IAPP and CGRP1/CALCA ligands (PubMed:35324283, PubMed:38603770)

Subcellular location

Cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6ZHOX-ray1.6 ÅA=24-111
8AX7X-ray1.65 ÅA=24-111
6ZISX-ray1.73 ÅA=24-111
7P0FX-ray1.85 ÅA=24-111
8AX6X-ray1.9 ÅA=24-111
6D1UX-ray2.05 ÅA/B/C=24-111
3N7SX-ray2.1 ÅC/D=26-117
7TYFEM2.2 ÅE=27-148
9BP3EM2.2 ÅE=27-148
7P0IX-ray2.3 ÅA=24-111
2YX8X-ray2.4 ÅA=27-112
9AUCEM2.4 ÅE=27-148
4RWGX-ray2.44 ÅA/B/C=23-108
6UMGX-ray2.7 ÅR/r=26-117
8AX5X-ray2.75 ÅA=24-111
3N7PX-ray2.8 ÅD/E/F/R=26-117
5V6YX-ray2.8 ÅA/B/C/D=24-111
3N7RX-ray2.9 ÅC/D=26-117
7TYWEM3.0 ÅE=27-148
7KNTEM3.15 ÅE=27-148

Showing 20 of 25 experimental structures (best resolution first).

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