Proteins

Proteins, proteomics

domains

A binding domain is that sequence of amino acids in a protein/protein family to which a specific ligand binds. As such, domains are vital to a protein's or enzyme's function. A structural domain is a self-stabilizing structural element that may fold independently of the rest of the protein chain.

Specific examples of domains:
cadherin repeats
carbohydrate-recognition domain (CRD)
caspase recruiting domains, CARD domains
C-lectin domain (CRD)
C-type-lectin-like domain (CTLD)
death domain (DD), death effector domain (DED) binds adaptor protein FADD (Fas-Associated Death Domain)
EF-hand domains
kringle domains
pleckstrin homology (PH) domain family
SH2 domain - Src homology 2 domain = p-Tyr recognition domains
zinc finger DNA binding domains

Others (on Wiki) Arginine Finger, Armadillo repeats, Basic Leucine zipper domain (bZIP domain), Phosphotyrosine-binding domain (PTB)

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kringle domains

Kringle domains, named for Scandinavian pastries, are conserved sequences that fold into large loops (stabilized by 3 disulfide linkages) the conformation of which is defined by hydrogen bonds and small pieces of anti-parallel β-sheet. Plasminogen-like kringles display affinity for free lysine and for lysine-containing peptides.

Kringle domains are found in several serine proteases, including prothrombin (with two kringle domains) and urokinase-type plasminogen activator, in ROR-like receptors, and they participate in protein-protein interactions with blood coagulation factors.

Urokinase-type plasminogen activator is a strong plasminogen activator which specifically cleaves the proenzyme/zymogen plasminogen to form the active enzyme plasmin.[s] Ror-family RTKs are characterized by the intracellular tyrosine kinase domains, highly related to those of the Trk-family RTKs, and by the extracellular Frizzled-like cysteine-rich domains (CRDs) and Kringle domains.[pm]

[] plasminogen, rotate human plasminogen, primary structure []

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. . . since 11/21/06