Calmodulin: Difference between revisions
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<StructureSection load='1cll' size='450' side='right' scene= caption='Human calmodulin complex with ethanol (PDB code [[1cll]])'> | <StructureSection load='1cll' size='450' side='right' scene='39/398280/Cv/3' caption='Human calmodulin complex with ethanol (PDB code [[1cll]])'> | ||
__TOC__ | __TOC__ | ||
==Function== | ==Function== | ||
Revision as of 12:07, 18 November 2015
FunctionCalmodulin (CaM) – calcium modulated protein – regulates various protein targets. It is used by various proteins as calcium sensor and signal transducer by binding to their calcium binding domain (CBD). It undergoes conformational change upon binding Ca++ via its 4 EF hand motives and can undergo post-translational modification. More details on apo-CaM in Calcium-free Calmodulin. Maximum Occurrence of Calmodulin ConformationsMaximum Occurrence, a method for making rigorous numerical assessments about the maximum percent of time that a conformer of a flexible macromolecule can exist and still be compatible with the experimental data, was used to probe the conformational disorder of Calmodulin[1]. ![]()
It was shown that the open (1cll) and closed (1prw) conformers can have MO of only 15% and 5% respectively. Calmodulin in MotionThe clip represents Calmodulin in motion. At the beginning it is shown moving in the unbound form (ApoCaM), and it changes its conformation when Calcium ions are present in the medium (CaCaM). Motion of ApoCaM is elaborated on the basis of 23 conformations derived from NMR file 1cfc, using the 3D animation program Blender, and according to a system to be published soon (Zini et al., manuscript in preparation). The transition from ApoCaM to CaCaM is elaborated with Blender starting with conformation 21 of 1cfc to arrive in conformation 11 of pdb file 1x02. Surface rendering is also elaborated using Blender, and shows the lipophilic potential as a scale of white-black and smooth-rough, form the most lipophilic to the hydrophilic. Electrostatic potential is represented as a series of lines moving in the direction Positive to Negative, elaborated according to a scheme to be published soon (Andrei et al., in preparation). As most lines are moving towards Calmodulin, one can learn that the protein is slightly acidic (negative partial charges on its surface). This movie was created by Andrei, Zini et al., of the Scientific Visualization Unit, Institute of Clinical Physiology - CNR of Itlay. Conformational change of Calmodulin
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3D Structures of Calmodulin
Updated on 18-November-2015
- Native CaM
- EF hand, Calcium-free Calmodulin – bCaM - bovine
- Maximum Occurrence – cCaM – chicken
- Maximum Occurrence, 1cll, 1prw – PtCaM - Paramecium tetraurelia
- 1cfc – rCaM - rat
- 1x02, 1dmo – XlCaM – NMR - Xenopus laevis
- 2k61, 2k0e – hCaM – NMR - human
- 1y6w, 1cll, 4bw8 - hCaM
- 4cln – DmCaM - Drosophila melanogaster
- 1rfj – CaM – potato
- 1ooj – CaM – Caenorhabditis elegans
- 4hex – mCaM – mouse
- EF hand, Calcium-free Calmodulin – bCaM - bovine
- Mutant CaM
- apo CaM
- CaM N-terminal
- CaM C-terminal
- 1f71 - XlCaM C-terminal – NMR
- 1cmg – bCaM C-terminal – NMR
- 1fw4 - bCaM C-terminal
- 1cmf – bapoCaM C-terminal – NMR
- 2hf5 - hCaM EF2 EF3 – NMR
- 2lqp - hCaM EF3 EF4 – NMR
- 2kxw – PtapoCaM + IQ motif of NAV1.2 – NMR
- 2m5e – PtCaM + Na channel protein
- 2kz2, 4bya – CaM (mutant) – chicken - NMR
- 2rrt – XlCaM (mutant)
- 1f71 - XlCaM C-terminal – NMR
- CaM+ cations (non calcium)
- CaM small molecule complexes
- CaM complexed with protein CBD domains
- 3gp2 – cCaM+CaM kinase II δ chain
- 2dfs – cCaM+myosin 5A
- 2o5g – cCaM+ myosin light chain kinase peptide
- 2bcx – cCaM+ryanodine receptor 1 peptide
- 3gof, 2o60 – cCaM+nitric oxide synthase CBD
- 1niw - rCaM+nitric oxide synthase CBD
- 2hqw - rCaM+glutamate receptor peptide
- 3bxk, 3bxl, 4ehq, 4j9y, 4j9z – rCaM+ calcium channel peptide
- 1g4y, 3sjq, 4g27, 4g28, 4qnh - rCaM+ potassium channel CBD
- 2ygg – rCaM + Na/H exchanger CBD
- 2mgu – rCaM + HIV-1 matrix protein CBD – NMR
- 1qx7 – rapoCaM+potassium channel peptide
- 4gow, 4umo, 4v0c – hCaM + potassium channel peptide
- 3hr4, 2ll6, 2ll7 - hCaM+nitric oxide synthase CBD
- 1yr5, 1wrz, 2y4v – hCaM+death-associated protein kinase 1 (DAP)
- 2l7l - hCaM+ CaM-dependent protein kinase 1 CBD
- 2m0j, 2m0k - hCaM+olfactory channel peptide
- 2kne – hCaM+PMCA C-terminal CBD
- 4upu - hCaM+ IP3 3-K CBD
- 3ewt, 3ewv – hCaM+TNFR fragment
- 2w73, 2jzi, 2r28 – hCaM+Ser/Thr phosphatase CBD
- 3bya – hCaM+glutamate receptor peptide
- 3g43, 2vay, 2f3y, 2f3z, 2be6, 2lqc, 3oxq – hCaM+calcium channel CAV1.2
- 3dve, 3dvj, 3dvk, 3dvm - hCaM+calcium channel CAV2.2
- 2k0f, 2lv6 – hCaM+myosin light chain kinase peptide – NMR
- 1zuz – hCaM+DRP kinase peptide
- 1l7z – hCaM+CAP-23/NAP-22 CBD
- 1cdl - hCaM+CaM dependent kinase CBD
- 1iwq - hCaM+MARCKS CBD
- 3sui – hCaM + capsaicin receptor peptide
- 2m55 – hCaM + α-synuclein peptide
- 2kn2 – sCaM C-terminal+NtMKP1 CBD – NMR
- 1cff - XlCaM+ calcium channel CBD - NMR
- 1sy9 – XlCaM+olfactory channel peptide
- 1nwd – XlCaM+glutamate decarboxylase CBD
- 1iq5 – XlCaM+CaM dependent kinase CBD
- 1ckk - XlCaM+CaM dependent kinase CBD - NMR
- 2llo, 2llq – XlCaM EF-hand domain + estrogen receptor CBD – NMR
- 2mes – XlCaM +PSD95 peptide - NMR
- 2mg5 - XlCaM+nitric oxide synthase peptide - NMR
- 2bbm, 2bbn - DmCaM+myosin light chain kinase peptide
- 1mxe – DmCaM+rCaMKI CBD
- 2fot - bCaM+α-II spectrin CBD
- 2f2o, 2f2p – bCaM+calcium
- 1xa5 – bCaM+KAR-2
- 1cm1, 1cm4, 1cdm - bCaM+CaM dependent kinase CBD
- 4e50 – mCam/linker/neurogranin IQ motif
- 4e53 – mCam/linker/neuromoduin IQ motif
- 4aqr – CaM-7 + calcium-transporting ATPase peptide – Arabidopsis thaliana
- 3gp2 – cCaM+CaM kinase II δ chain
- Calmodulin complex with protein
- 2col, 1yrt, 1yru – BpCaM+adenyl cyclase – Bordetella pertussis
- 1zot – BpCaM C-terminal+adenyl cyclase
- 1xfu, 1xfv, 1xfw, 1xfx, 1xfy, 1xfz, 1y0v, 1sk6, 1pk0, 1lvc, 1k90, 1k93 - CaM+adenyl cyclase – Bacillus anthracis
- 2l1w – CaM+vacuolar calcium ATPase peptide – soybean – NMR
- 2lgf – hCaM + selectin peptide
- 3j41 – hCaM + lens fiber major intrinsic protein – Cryo EM
- 2vas, 2vb6, 3gn4, 3l9i, 4dbp, 4dbq, 2x51, 4anj – DmCaM+pMyosin IV
- 1qs7, 1qtx – CaM+RS20 – Escherichia coli
- 1vrk – CaM (mutant)+RS20
- 3ek4, 3ek7, 3ek8, 3ekh, 3ekj, 3evr, 3evu, 3evv, 3o77, 3o78 – CaM/DFP/myosin light chain kinase
- 4ds7 – CaM + spindle pole body component 10 – Kluyveromyces lactis
- 2dfs – cCaM+myosin 5A
- 4l79, 4byf – hCaM + myosin 1B
- 4r8g – rCaM + myosin 1B
- 2x0g – hCaM+death-associated protein kinase 1 (DAP)
- 4djc, 2l53, 4ovn - hCaM+ sodium channel protein type V α subunit
- 4dck, 4jpz - hCaM+ sodium channel protein type V α subunit + fibroblast growth factor 13
- 4jq0 - hCaM+ sodium channel protein type V α subunit + fibroblast growth factor 12
- 2x51, 4anj – DmCaM+pMyosin IV
- 2k3s – CaM+smoothelin-like protein 1 – NMR
- 2ix7 – apoCaM+myosin-5A
- 2bki, 2bkh – CaM+myosin VI – pig
- 4lzx, 4m1l - hCaM+ IQ domain-containing protein G
- 4q57 – hCaM N-terminal + plectin
- 4q5u – hCaM + calcineurin
- 2col, 1yrt, 1yru – BpCaM+adenyl cyclase – Bordetella pertussis
See Also
Bibliography
Proteopedia Page Contributors and Editors (what is this?)
Alexander Berchansky, Karsten Theis, Enrico Ravera, Daniel Moyano-Marino, Jaime Prilusky, Michal Harel
