Structural domain
Structural domain refers to a part of a protein that is self-stabilizing and can fold independently of the rest. This term represents a unit of tertiary structure that can exist or fold independently, and is often associated with a specific function.
Overview[edit | edit source]
The concept of a domain arises from observations that many proteins are composed of several discrete, independent units or modules. These units are capable of folding into stable structures that often have associated functions. The term domain is often used to describe such units.
Structure[edit | edit source]
Structural domains are parts of the protein's overall tertiary structure that can self-stabilize and fold independently of the rest of the protein chain. These domains often fold into distinct structural motifs, such as alpha helices and beta sheets.
Function[edit | edit source]
Domains often have specific functions, independent of the rest of the protein chain. For example, they may serve as enzyme active sites, or provide binding sites for other molecules or ions. Some domains are responsible for the regulation of protein activity, while others may have structural roles.
Classification[edit | edit source]
Structural domains can be classified into families based on their sequence and structure similarities. These families can be further grouped into superfamilies and folds. The Structural Classification of Proteins (SCOP) and CATH are two commonly used classification systems.
See also[edit | edit source]
Structural domain Resources | |
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Contributors: Prab R. Tumpati, MD