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2bbm
From Proteopedia
| 2bbm, 1 NMR models () | |||||||||
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| Sites: | , , and | ||||||||
| Ligands: | |||||||||
| Related: | 2bbn | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULTIDIMENSIONAL NMR
The three-dimensional solution structure of the complex between calcium-bound calmodulin (Ca(2+)-CaM) and a 26-residue synthetic peptide comprising the CaM binding domain (residues 577 to 602) of skeletal muscle myosin light chain kinase, has been determined using multidimensional heteronuclear filtered and separated nuclear magnetic resonance spectroscopy. The two domains of CaM (residues 6 to 73 and 83 to 146) remain essentially unchanged upon complexation. The long central helix (residues 65 to 93), however, which connects the two domains in the crystal structure of Ca(2+)-CaM, is disrupted into two helices connected by a long flexible loop (residues 74 to 82), thereby enabling the two domains to clamp residues 3 to 21 of the bound peptide, which adopt a helical conformation. The overall structure of the complex is globular, approximating an ellipsoid of dimensions 47 by 32 by 30 angstroms. The helical peptide is located in a hydrophobic channel that passes through the center of the ellipsoid at an angle of approximately 45 degrees with its long axis. The complex is mainly stabilized by hydrophobic interactions which, from the CaM side, involve an unusually large number of methionines. Key residues of the peptide are Trp4 and Phe17, which serve to anchor the amino- and carboxyl-terminal halves of the peptide to the carboxyl- and amino-terminal domains of CaM, respectively. Sequence comparisons indicate that a number of peptides that bind CaM with high affinity share this common feature containing either aromatic residues or long-chain hydrophobic ones separated by a stretch of 12 residues, suggesting that they interact with CaM in a similar manner.
Solution structure of a calmodulin-target peptide complex by multidimensional NMR., Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A, Science. 1992 May 1;256(5057):632-8. PMID:1585175
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2bbm is a 2 chain structure of Calmodulin with sequence from Drosophila melanogaster. The August 2003 RCSB PDB Molecule of the Month feature on Calmodulin by Shuchismita Dutta and David S. Goodsell is 10.2210/rcsb_pdb/mom_2003_8. Full experimental information is available from OCA.
See Also
Reference
- Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science. 1992 May 1;256(5057):632-8. PMID:1585175
