immunoglobulin domain

Proposed start points for immunoglobulin domains are indicated above the nucleotide sequence.

Ultimately, alpha-1B glycoprotein seems to be primarily composed of four immunoglobulin domains.

Each light chain is composed of two tandem immunoglobulin domains:

There is a large segment of amino acids from position 297 to 400 that is not shown to be an immunoglobulin domain.

The variable domain of any heavy chain is composed of a single immunoglobulin domain.

Human genes encoding proteins containing the immunoglobulin domain include:

This linker region establishes a second class for connections between unpaired immunoglobulin domains, the characteristics of which are shown in Fig.3 d.

It has two C2-set immunoglobulin domains, and it's probable that the binding site for its ligand is near the interdomain hinge.

Rigid-body refinement (as implemented in X-plor) was used to define precisely the position and orientation of each separate immunoglobulin domain.

It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail.

It consists of two extramembrane immunoglobulin domains, which are associated with extracellular glycosylated mucine and together they form a stalk.

It has four immunoglobulin domains (D to D) that are exposed on the extracellular surface of the cell:

V-set and immunoglobulin domain containing 2 is a protein in humans that is encoded by the VSIG2 gene.

Alignment of immunoglobulin domains between ICAM-3 and ICAMs 1 and 2.

The immunoglobulin superfamily is large and diverse probably because the basic structure of the immunoglobulin domain is versatile and readily adaptable to different binding functions.

The leukocyte immunoglobulin-like receptors (LILR) are a family of receptors possessing extracellular immunoglobulin domains.

All nectins and all Necls share the same overall structure defined by three extra cellular immunoglobulin domains, a single transmembrane helix and an intracellular domain.

These have been shown to align to the 43 nm axial repeats of myosin thick filaments with immunoglobulin domains correlating to myosin crowns.

An initial NCBI Blast alignment of alpha-1B glycoprotein illustrates that the protein is mainly composed of three immunoglobulin domains.

PDGF binds to PDGFRs ligand binding pocket located within the second and third immunoglobulin domains.

The LRRN3 protein also has an immunoglobulin domain, a fibronectin type III domain, and a transmembrane region toward the end of the protein.

Each Siglec contains an N-terminal V-type immunoglobulin domain (Ig domain) which acts as the binding receptor for sialic acid.

The CD3γ, CD3δ, and CD3ε chains are highly related cell-surface proteins of the immunoglobulin superfamily containing a single extracellular immunoglobulin domain.

The VCAM-1 gene contains six or seven immunoglobulin domains, and is expressed on both large and small blood vessels only after the endothelial cells are stimulated by cytokines.

However, a NCBI BLAST alignment of just the amino acids from 297-400 does illustrate that the latter sequence is indeed a fourth immunoglobulin domain.