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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Introduction

Diabetes

Function

^[3].

Disease

Relevance

Structural highlights

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Binding/Active Site of GIPR with GIP

Figure 1. GIPR and GIP residue interactions

The of GIP with the GIP receptor (GIPR) is where the N-term of GIP binds with the transmembrane domain of the GIPR. The first interaction formed with GIPR and the N-term of GIP is a hydrogen bond between Tyrosine 1 (Y1) and Glutamine 224 (Q224) to activate the G-protein to start sending signals to the cell. Many other within the binding site are forming hydrogen bonds and hydrophobic interactions between the ligand and the receptor. The N-term binds more strongly than the C-term and there are many different residues contributing to this, including, Tyrosine 1 (Y1) and Tryptophan (W296) are forming aromatic interactions. Serine 8 (S8) and Asparagine 290 (N290) are forming two hydrogen bonds with each other. Aspartate 9 (D9) is forming another hydrogen bond with Arginine 370 (R370)Cite error: Invalid <ref> tag; refs with no content must have a name. These hydrogen bonds lead to the activation of cell signaling and when this binding is somehow disrupted, that is what causes different diseases like diabetes.

Binding/Active Site of GIPR with Tirzepatide

Figure 2. Residue Interactions with Tirzepatide

The is the same as GIP with the N-term binding to the extracellular membrane. The are mostly the same just in a different conformation that is allowing for more hydrogen bonding.

Isoleucine vs. Threonine