Structural Patterns within Tertiary Structure and PTMs

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10 Terms

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Structural Patterns within Tertiary Structure

Motif/Fold and Domains

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Motif or Fold

A common folding pattern involving two or more elements of secondary structure and the connections between them

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Domains

Regions of tertiary structure that are independently stable and often have unique functions

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Posttranslational Modification of Proteins PTMs

Most proteins are chemically modified after they are synthesized within a cell

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Why PTMs

Increases chemical diversity. Enables regulation of protein activity.

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Phosphorylation

Addition of a phosphate to Ser Thr or Tyr. Often causes a conformational change regulating protein activity. Catalyzed by kinases and phosphatases.

<p>Addition of a phosphate to Ser Thr or Tyr. Often causes a conformational change regulating protein activity. Catalyzed by<strong> kinases</strong> and <strong>phosphatases.</strong></p>
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Glycosylation

Addition of a carbohydrate to Ser Thr (O linked) or Asn (N linked). Common among extracellular and secreted proteins. Catalyzed by glycosyltransferases and glycosidases

<p>Addition of a carbohydrate to Ser Thr (O linked) or Asn (N linked). Common among extracellular and secreted proteins. Catalyzed by <strong>glycosyltransferases</strong> and <strong>glycosidases</strong></p>
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Acetylation

Addition of an acetyl group to Lys or protein N termini. Diverse functions including regulation of gene expression. Catalyzed by deacetylases and acetyltransferases

<p>Addition of an acetyl group to Lys or protein N termini. Diverse functions including regulation of gene expression. Catalyzed by <strong>deacetylases</strong> and <strong>acetyltransferases</strong></p>
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Prenylation

Addition of a prenyl group to Cys. Targets protein to membranes. Catalyzed by farnesyl transferase or geranylgeranyl transferase

<p>Addition of a prenyl group to Cys. Targets protein to membranes. Catalyzed by<strong> farnesyl transferase </strong>or <strong>geranylgeranyl transferase</strong></p>
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Proteolysis

Many protein are cleaved by proteolysis to their active form. The inactive precursors are called proproteins. Irreversible

<p>Many protein are cleaved by proteolysis to their active form. The inactive precursors are called <strong>proproteins</strong>. Irreversible</p>

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