1deg
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1deg.gif|left|200px]] | + | [[Image:1deg.gif|left|200px]] |
- | + | ||
- | '''THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE''' | + | {{Structure |
+ | |PDB= 1deg |SIZE=350|CAPTION= <scene name='initialview01'>1deg</scene>, resolution 2.9Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
- | 1DEG is a [ | + | 1DEG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEG OCA]. |
==Reference== | ==Reference== | ||
- | The linker of des-Glu84-calmodulin is bent., Raghunathan S, Chandross RJ, Cheng BP, Persechini A, Sobottka SE, Kretsinger RH, Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6869-73. PMID:[http:// | + | The linker of des-Glu84-calmodulin is bent., Raghunathan S, Chandross RJ, Cheng BP, Persechini A, Sobottka SE, Kretsinger RH, Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6869-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8341712 8341712] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 25: | Line 34: | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:15 2008'' |
Revision as of 08:37, 20 March 2008
| |||||||
, resolution 2.9Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | |||||||
Coordinates: | save as pdb, mmCIF, xml |
THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE
Contents |
Overview
The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether.
Disease
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]
About this Structure
1DEG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The linker of des-Glu84-calmodulin is bent., Raghunathan S, Chandross RJ, Cheng BP, Persechini A, Sobottka SE, Kretsinger RH, Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6869-73. PMID:8341712
Page seeded by OCA on Thu Mar 20 10:37:15 2008