Complete 1H, 13C, and 15N assignments and secondary structure of the GTPase activating domain of Gs.

Source:http://linkedlifedata.com/resource/pubmed/id/7819191

Biochemistry 1995 Jan 10 34 1 155-62

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General Info

Authors

Bourne HR, Benjamin DR, Kuntz ID, Markby DW

Affiliation

Department of Pharmaceutical Chemistry, University of California at San Francisco 94143.

Abstract

Complete 1H, 13C, and 15N assignments for backbone and side-chain atoms of the 145 residue GTPase activating domain of Gs are presented. The combination of gradient-enhanced versions of the HNCACB and CBCA(CO)NNH pulse sequences provided enough information to obtain sequential backbone assignments for residues 2-145 of the polypeptide, as well as assignments of asparagine and glutamine side-chain amides. HBHA(CO)NNH, HCCH-TOCSY, and 13C/15N NOESY-HSQC experiments yielded side-chain 1H and 13C assignments. Chemical shift data and 15N NOESY-HSQC experiments provided information on the secondary structure of the domain, which is similar to that observed in the cognate domain in transducin, a related G protein. The functionally essential C-terminal 15 residues are disordered in solution. These assignments provide a basis for determining the solution structure of the domain.

PMID
7819191

Publication types

Research Support, U.S. Gov't, P.H.S.; Research Support, Non-U.S. Gov't