Motion in Various Kinases (Tyr, Ser, Thr) [erk2]

[ jump to morphs ]

Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures 1ERK MAP Kinase [ PartsList ] 1IRK Domain from insulin receptortyrosine kinase [ PartsList ] 1KOB twitchin Kinase [ PartsList ]

Description Has a similar motion to cAMP-dependent protein kinase (pka) but only solved in one conformation. According to Hubbard et al. paper, N-terminal domain of tyrosine kinase (IRK) is rotated 26 degrees and translated 0.8 A relative to closed form of pka and 19 and 2.1 relative to open form. MAP Kinase and twitchin adopt more open conformations with rotations relative to the open form of pka of 17 and 30 degrees, respectively.

Particular values describing motion Experimental Methods = x (Traditional x-ray) Creation Date = 19970822 Modification Date = 19971214

References F Zhang, A Strand, D Robbins, M Cobb and E J Goldsmith (1994). Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature. 367: 704-710. [Medline info for 94150699] Hubbard SR; Wei L; Ellis L; Hendrickson WA (1994). Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372: 746-54. [Medline info for 95089813] Morgan DO, De Bondt HL (1994). Protein kinase regulation: insights from crystal structure analysis. Curr Opin Cell Biol. 6(2):239-246. [Medline info for 94296697]

GO terms associated with structures Molecular function transmembrane receptor protein tyrosine kinase activity, MAP kinase activity, epidermal growth factor receptor activity, ATP binding, protein kinase activity, protein-tyrosine kinase activity, protein serine/threonine kinase activity Cellular component membrane Biological process transmembrane receptor protein tyrosine kinase signaling pathway, protein amino acid phosphorylation

Morphs

[ show all images ]

Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

---

Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu