View source for 1cll

[[Image:1cll.gif|left|200px]]

 {{Structure
|PDB= 1cll |SIZE=350|CAPTION= <scene name='initialview01'>1cll</scene>, resolution 1.7&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>
|ACTIVITY= 
|GENE= 
}}

'''CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION'''


==Overview==
We have determined and refined the crystal structure of a recombinant calmodulin at 1.7 A resolution. The structure was determined by molecular replacement, using the 2.2 A published native bovine brain structure as the starting model. The final crystallographic R-factor, using 14,469 reflections in the 10.0 to 1.7 A range with structure factors exceeding 0.5 sigma, is 0.216. Bond lengths and bond angle distances have root-mean-square deviations from ideal values of 0.009 A and 0.032 A, respectively. The final model consists of 1279 non-hydrogen atoms, including four calcium ions, 1130 protein atoms, including three Asp118 side-chain atoms in double conformation, 139 water molecules and one ethanol molecule. The electron densities for residues 1 to 4 and 148 of calmodulin are poorly defined, and not included in our model, except for main-chain atoms of residue 4. The calmodulin structure from our crystals is very similar to the earlier 2.2 A structure described by Babu and coworkers with a root-mean-square deviation of 0.36 A. Calmodulin remains a dumb-bell-shaped molecule, with similar lobes and connected by a central alpha-helix. Each lobe contains three alpha-helices and two Ca2+ binding EF hand loops, with a short antiparallel beta-sheet between adjacent EF hand loops and one non-EF hand loop. There are some differences in the structure of the central helix. The crystal packing is extensively studied, and facile crystal growth along the z-axis of the triclinic crystals is explained. Herein, we describe hydrogen bonding in the various secondary structure elements and hydration of calmodulin.

==Disease==
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604214 604214]], Cerebral cavernous malformations-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604214 604214]], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604214 604214]], Leukemia, acute T-cell lymphoblastic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603025 603025]], Leukemia, acute myeloid OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603025 603025]]

==About this Structure==
1CLL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1CLL with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb44_1.html Calmodulin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLL OCA]. 

==Reference==
Calmodulin structure refined at 1.7 A resolution., Chattopadhyaya R, Meador WE, Means AR, Quiocho FA, J Mol Biol. 1992 Dec 20;228(4):1177-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1474585 1474585]
[[Category: Calmodulin]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Chattopadhyaya, R.]]
[[Category: Quiocho, F A.]]
[[Category: CA]]
[[Category: EOH]]
[[Category: calcium-binding protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:53 2008''