1deg

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==Overview==
==Overview==
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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.
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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==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chandross, R.]]
[[Category: Chandross, R.]]
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[[Category: Cheng, B.P.]]
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[[Category: Cheng, B P.]]
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[[Category: Kretsinger, R.H.]]
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[[Category: Kretsinger, R H.]]
[[Category: Persechini, A.]]
[[Category: Persechini, A.]]
[[Category: Raghunathan, S.]]
[[Category: Raghunathan, S.]]
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[[Category: Sobottk, S.E.]]
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[[Category: Sobottk, S E.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:39:26 2008''
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''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


1deg, resolution 2.9Å

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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

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