PMID- 10074346
OWN - NLM
STAT- MEDLINE
DCOM- 19990323
LR  - 20131121
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 38
IP  - 10
DP  - 1999 Mar 9
TI  - Conformational changes in fragments D and double-D from human fibrin(ogen) upon
      binding the peptide ligand Gly-His-Arg-Pro-amide.
PG  - 2941-6
AB  - The structure of fragment double-D from human fibrin has been solved in the
      presence and absence of the peptide ligands that simulate the two knobs exposed
      by the removal of fibrinopeptides A and B, respectively. All told, six crystal
      structures have been determined, three of which are reported here for the first
      time: namely, fragments D and double-D with the peptide GHRPam alone and double-D
      in the absence of any peptide ligand. Comparison of the structures has revealed a
      series of conformational changes that are brought about by the various knob-hole 
      interactions. Of greatest interest is a moveable "flap" of two negatively charged
      amino acids (Glubeta397 and Aspbeta398) whose side chains are pinned back to the 
      coiled coil with a calcium atom bridge until GHRPam occupies the beta-chain
      pocket. Additionally, in the absence of the peptide ligand GPRPam, GHRPam binds
      to the gamma-chain pocket, a new calcium-binding site being formed concomitantly.
FAU - Everse, S J
AU  - Everse SJ
AD  - Center for Molecular Genetics, University of California, San Diego, La Jolla
      92093-0634, USA.
FAU - Spraggon, G
AU  - Spraggon G
FAU - Veerapandian, L
AU  - Veerapandian L
FAU - Doolittle, R F
AU  - Doolittle RF
LA  - eng
SI  - PDB/1FZE
SI  - PDB/1FZF
SI  - PDB/1FZG
GR  - HL-26873/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Fibrin Fibrinogen Degradation Products)
RN  - 0 (Ligands)
RN  - 0 (Oligopeptides)
RN  - 0 (Peptide Fragments)
RN  - 0 (fibrinogen D fragment)
RN  - 67869-60-7 (glycyl-histidyl-arginyl-proline)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Binding Sites
MH  - Calcium/physiology
MH  - Calcium-Binding Proteins/metabolism
MH  - Computer Simulation
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - Fibrin Fibrinogen Degradation Products/*chemistry/*metabolism
MH  - Humans
MH  - Ligands
MH  - Models, Molecular
MH  - Oligopeptides/*metabolism
MH  - Peptide Fragments/chemistry
MH  - Protein Binding
MH  - Protein Conformation
EDAT- 1999/03/13 00:00
MHDA- 1999/03/13 00:01
CRDT- 1999/03/13 00:00
PHST- 1999/03/13 00:00 [pubmed]
PHST- 1999/03/13 00:01 [medline]
PHST- 1999/03/13 00:00 [entrez]
AID - 10.1021/bi982626w [doi]
AID - bi982626w [pii]
PST - ppublish
SO  - Biochemistry. 1999 Mar 9;38(10):2941-6. doi: 10.1021/bi982626w.