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dackerin

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There are 8 letters in DACKERIN ( A¹C³D²E¹I¹K⁵N¹R¹ )

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5 letters out of DACKERIN

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3 letters out of DACKERIN

ACE AID AIN AIR AND ANE ANI ARC ARE ARK CAD CAN CAR DAK DAN DEN DIE DIN EAR END ERA ERN ICE ICK INK IRE IRK KAE KEA KEN KID KIN KIR NAE RAD RAI RAN REC RED REI RIA RID RIN

2 letters out of DACKERIN

AD AE AI AN AR DE ED EN ER ID IN KA KI NA NE RE

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Dackerin might refer to
Dockerin is a protein domain found in the cellulosome cellular structure of anaerobic bacteria. It is found on many endoglucanase enzymes. The dockerin's binding partner is the cohesin domain, located on the scaffoldin protein. This interaction between the dockerin domains of the enzyme constituents of the cellulosome and the cohesin domains of the scaffoldin protein is essential to the construction of the cellulosome complex. The Dockerin domain has two in-tandem repeats of a non-EF hand calcium binding motif. Each motif is characterized by a loop-helix structure. The three-dimensional structure of dockerin has been determined in solution, as well as in complex with Cohesin.There are three types of Dockerin domains: I, II and III which bind to Cohesin Type I, Cohesin Type II and Cohesin Type III respectively. A type I dockerin domain is 65-70 residues long. The binding specificity of Type I interaction was well studied by structural and mutagenesis studies. Type II interaction is less well characterized.

Dackerin might refer to

Dockerin is a protein domain found in the cellulosome cellular structure of anaerobic bacteria. It is found on many endoglucanase enzymes. The dockerin's binding partner is the cohesin domain, located on the scaffoldin protein. This interaction between the dockerin domains of the enzyme constituents of the cellulosome and the cohesin domains of the scaffoldin protein is essential to the construction of the cellulosome complex. The Dockerin domain has two in-tandem repeats of a non-EF hand calcium binding motif. Each motif is characterized by a loop-helix structure. The three-dimensional structure of dockerin has been determined in solution, as well as in complex with Cohesin.There are three types of Dockerin domains: I, II and III which bind to Cohesin Type I, Cohesin Type II and Cohesin Type III respectively. A type I dockerin domain is 65-70 residues long. The binding specificity of Type I interaction was well studied by structural and mutagenesis studies. Type II interaction is less well characterized.

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