This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2h43

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 2h43 |SIZE=350|CAPTION= <scene name='initialview01'>2h43</scene>, resolution 2.7&Aring;
|PDB= 2h43 |SIZE=350|CAPTION= <scene name='initialview01'>2h43</scene>, resolution 2.7&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
+
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1fzg|1FZG]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h43 OCA], [http://www.ebi.ac.uk/pdbsum/2h43 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h43 RCSB]</span>
}}
}}
Line 14: Line 17:
==Overview==
==Overview==
The beta-chain amino-terminal sequences of all known mammalian fibrins begin with the sequence Gly-His-Arg-Pro- (GHRP-), but the homologous sequence in chicken fibrin begins with the sequence Ala-His-Arg-Pro- (AHRP-). Nonetheless, chicken fibrinogen binds the synthetic peptide GHRPam, and a previously reported crystal structure has revealed that the binding is in exact conformance with that observed for the human GHRPam-fragment D complex. We now report that human fibrinogen, which is known not to bind APRP, binds the synthetic peptide AHRPam. Moreover, a crystal structure of AHRPam complexed with fragment D from human fibrinogen shows that AHRPam binds exclusively to the beta-chain hole and, unlike GHRPam, not at all to the homologous gamma-chain hole. The difference can be attributed to the methyl group of the alanine residue clashing with a critical carboxyl group in the gammaC hole but being accommodated in the roomier betaC hole where the equivalent carboxyl is situated more flexibly.
The beta-chain amino-terminal sequences of all known mammalian fibrins begin with the sequence Gly-His-Arg-Pro- (GHRP-), but the homologous sequence in chicken fibrin begins with the sequence Ala-His-Arg-Pro- (AHRP-). Nonetheless, chicken fibrinogen binds the synthetic peptide GHRPam, and a previously reported crystal structure has revealed that the binding is in exact conformance with that observed for the human GHRPam-fragment D complex. We now report that human fibrinogen, which is known not to bind APRP, binds the synthetic peptide AHRPam. Moreover, a crystal structure of AHRPam complexed with fragment D from human fibrinogen shows that AHRPam binds exclusively to the beta-chain hole and, unlike GHRPam, not at all to the homologous gamma-chain hole. The difference can be attributed to the methyl group of the alanine residue clashing with a critical carboxyl group in the gammaC hole but being accommodated in the roomier betaC hole where the equivalent carboxyl is situated more flexibly.
- 
-
==Disease==
 
-
Known diseases associated with this structure: Afibrinogenemia, congenital OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Afibrinogenemia, congenital OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134830 134830]], Amyloidosis, hereditary renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134820 134820]], Dysfibrinogenemia, beta type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134830 134830]], Dysfibrinogenemia, gamma type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134850 134850]], Hypofibrinogenemia, gamma type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134850 134850]], Thrombophilia, dysfibrinogenemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134830 134830]], Thrombophilia, dysfibrinogenemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134850 134850]]
 
==About this Structure==
==About this Structure==
Line 27: Line 27:
[[Category: Doolittle, R F.]]
[[Category: Doolittle, R F.]]
[[Category: Pandi, L.]]
[[Category: Pandi, L.]]
-
[[Category: CA]]
 
-
[[Category: NH2]]
 
[[Category: coiled-coil]]
[[Category: coiled-coil]]
[[Category: fragment d]]
[[Category: fragment d]]
[[Category: knob-hole interaction]]
[[Category: knob-hole interaction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:12:21 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:25:11 2008''

Revision as of 00:25, 31 March 2008


PDB ID 2h43

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands: , , ,
Related: 1FZG


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide


Overview

The beta-chain amino-terminal sequences of all known mammalian fibrins begin with the sequence Gly-His-Arg-Pro- (GHRP-), but the homologous sequence in chicken fibrin begins with the sequence Ala-His-Arg-Pro- (AHRP-). Nonetheless, chicken fibrinogen binds the synthetic peptide GHRPam, and a previously reported crystal structure has revealed that the binding is in exact conformance with that observed for the human GHRPam-fragment D complex. We now report that human fibrinogen, which is known not to bind APRP, binds the synthetic peptide AHRPam. Moreover, a crystal structure of AHRPam complexed with fragment D from human fibrinogen shows that AHRPam binds exclusively to the beta-chain hole and, unlike GHRPam, not at all to the homologous gamma-chain hole. The difference can be attributed to the methyl group of the alanine residue clashing with a critical carboxyl group in the gammaC hole but being accommodated in the roomier betaC hole where the equivalent carboxyl is situated more flexibly.

About this Structure

2H43 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Differences in binding specificity for the homologous gamma- and beta-chain "holes" on fibrinogen: exclusive binding of Ala-His-Arg-Pro-amide by the beta-chain hole., Doolittle RF, Chen A, Pandi L, Biochemistry. 2006 Nov 28;45(47):13962-9. PMID:17115691

Page seeded by OCA on Mon Mar 31 03:25:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools