PMID- 7756251 OWN - NLM STAT- MEDLINE DCOM- 19950629 LR - 20190613 IS - 0006-2960 (Print) IS - 0006-2960 (Linking) VI - 34 IP - 19 DP - 1995 May 16 TI - The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. PG - 6261-6 AB - Modern NMR methods were used to determine the secondary structure topology of the 18 kDa peptide binding domain of the chaperone protein Hsc70 in solution. This report constitutes the first experimental conformational information on this important domain of the class of Hsp70 proteins. The domain consists of two four-stranded antiparallel beta-sheets and a single alpha-helix. The topology does not resemble at all the topology observed in the human leukocyte antigen (HLA) proteins of the major histocompatibility complex. This is significant because such resemblance was predicted on the basis of limited amino acid homology, secondary structure prediction, and related function. Moreover, the exact meander-type beta-sheet topology identified in Hsc70 has to our best knowledge not been observed in any other known protein structure. FAU - Morshauser, R C AU - Morshauser RC AD - Department of Biological Chemistry, University of Michigan, Ann Arbor 48109, USA. FAU - Wang, H AU - Wang H FAU - Flynn, G C AU - Flynn GC FAU - Zuiderweg, E R AU - Zuiderweg ER LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, Non-P.H.S. PT - Research Support, U.S. Gov't, P.H.S. PL - United States TA - Biochemistry JT - Biochemistry JID - 0370623 RN - 0 (Carrier Proteins) RN - 0 (HSC70 Heat-Shock Proteins) RN - 0 (HSP70 Heat-Shock Proteins) RN - 0 (Hspa8 protein, rat) RN - 0 (Molecular Chaperones) RN - 0 (Peptides) SB - IM MH - Amino Acid Sequence MH - Animals MH - Binding Sites MH - Carrier Proteins/*chemistry MH - HSC70 Heat-Shock Proteins MH - *HSP70 Heat-Shock Proteins MH - Hydrogen Bonding MH - Magnetic Resonance Spectroscopy MH - Molecular Chaperones/*chemistry MH - Molecular Sequence Data MH - Peptides/metabolism MH - Protein Structure, Secondary MH - Rats EDAT- 1995/05/16 00:00 MHDA- 1995/05/16 00:01 CRDT- 1995/05/16 00:00 PHST- 1995/05/16 00:00 [pubmed] PHST- 1995/05/16 00:01 [medline] PHST- 1995/05/16 00:00 [entrez] AID - 10.1021/bi00019a001 [doi] PST - ppublish SO - Biochemistry. 1995 May 16;34(19):6261-6. doi: 10.1021/bi00019a001.