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| {{STRUCTURE_1qfh| PDB=1qfh | SCENE= }} | | {{STRUCTURE_1qfh| PDB=1qfh | SCENE= }} |
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| '''DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6'''
| | ===DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6=== |
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| ==Overview==
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| Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. The extended molecule has an N-terminal 250-residue actin-binding domain and a rod constructed from six 100-residue repeats that have an Ig fold. The ability to dimerize is crucial to the actin cross-linking function of gelation factor and is mediated by the rod in which the two chains are arranged in an antiparallel fashion. We report the 2.2 A resolution crystal structure of rod domains 5 and 6, which shows that dimerization is mediated primarily by rod domain 6 and is the result of a double edge-to-edge extension of beta-sheets. Thus, contrary to earlier proposals, the chains of the dimeric gelation factor molecule overlap only within domain 6, and domains 1-5 do not pair with domains from the other chain. This information allows construction of a model of the gelation factor molecule and suggests how the chains in the related molecule filamin (ABP280) may interact.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10467095}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10467095 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10467095}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Gelation factor]] | | [[Category: Gelation factor]] |
| [[Category: Immunoglobulin]] | | [[Category: Immunoglobulin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:12:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:44:12 2008'' |