Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin

Journal Article · Tue Oct 22 00:00:00 EDT 1991 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00106a003· OSTI ID:5617875

Roth, S M; Schneider, D M; Wand, A J ^[1]; Strobel, L A ^[2]; VanBerkum, M F.A.; Means, A R ^[3]

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1. Fox Chase Cancer Center, Philadelphia, PA (United States) Univ. of Illinois, Urbana (United States)
2. Fox Chase Cancer Center, Philadelphia, PA (United States)
3. Baylor College of Medicine, Houston, TX (United States)

The interaction between the peptide corresponding to the calmodulin-binding domain of smooth muscle myosin light-chain kinase and (Ca{sup 2+}){sub 4}-calmodulin has been studied by multinuclear and multidimensional nuclear magnetic resonance methods. The study was facilitated by the use of {sup 15}N-labeled peptide in conjunction with {sup 15}N-edited and {sup 15}N-correlated {sup 1}H spectroscopy. The peptide forms a 1:1 complex with calcium-saturated calmodulin which is in slow exchange with free peptide. The {sup 1}H and {sup 15}N resonances of the bound have been assigned. An extensive set of structural constraints for the bound peptide has been assembled from the analysis of nuclear Overhauser effects and three-bond coupling constants. The backbone conformation of the bound peptide has been determined using these constraints by use of distance geometry and related computational methods. The backbone conformation of the peptide has been determined to high precision and is generally indicative of helical secondary structure. Nonhelical backbone conformations are seen in the middle and at the C-terminal end of the bound peptide. These studies provide the first direct confirmation of the amphiphilic helix model for the structure of peptides bound to calcium-saturated calmodulin.

• OSTI ID: 5617875
• Journal Information: Biochemistry; (United States), Vol. 30:42; ISSN 0006-2960
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
CALMODULIN
NUCLEAR MAGNETIC RESONANCE
PEPTIDES
CONFORMATIONAL CHANGES
RECEPTORS
MUSCLES
MYOSIN
NITROGEN 15
OVERHAUSER EFFECT
PHOSPHOTRANSFERASES
PROTONS
BARYONS
ELEMENTARY PARTICLES
ENZYMES
FERMIONS
GLOBULINS
HADRONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MEMBRANE PROTEINS
NITROGEN ISOTOPES
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
PROTEINS
RESONANCE
STABLE ISOTOPES
TRANSFERASES
550201* - Biochemistry- Tracer Techniques