1deg
From Proteopedia
Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
- | The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been | + | 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== | ==Disease== | ||
Line 17: | Line 17: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chandross, R.]] | [[Category: Chandross, R.]] | ||
- | [[Category: Cheng, B | + | [[Category: Cheng, B P.]] |
- | [[Category: Kretsinger, R | + | [[Category: Kretsinger, R H.]] |
[[Category: Persechini, A.]] | [[Category: Persechini, A.]] | ||
[[Category: Raghunathan, S.]] | [[Category: Raghunathan, S.]] | ||
- | [[Category: Sobottk, S | + | [[Category: Sobottk, S E.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:49 2008'' |
Revision as of 10:15, 21 February 2008
|
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 with as ligand. 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 Feb 21 12:15:49 2008